P0C6V6 (R1A_PEDV7) 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 epidemic diarrhea virus (strain CV777) (PEDV) [Complete proteome]

Taxonomic identifier

229032 [NCBI]

Taxonomic lineage

Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Nidovirales › Coronaviridae › Coronavirinae › Alphacoronavirus › Porcine epidemic diarrhea virus

Virus host

Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	4117 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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-|-[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. 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. 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.
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 and PL-PRO proteinases are autocatalytically processed By similarity.
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	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
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: P0C6V6-1)

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: P0C6Y4-1)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 4117	4117	Replicase polyprotein 1a		PRO_0000338347
	Chain	1 – 110	110	Non-structural protein 1 By similarity		PRO_0000338348
	Chain	111 – 895	785	Non-structural protein 2 By similarity		PRO_0000338349
	Chain	896 – 2516	1621	Non-structural protein 3 By similarity		PRO_0000338350
	Chain	2517 – 2997	481	Non-structural protein 4 By similarity		PRO_0000338351
	Chain	2998 – 3299	302	3C-like proteinase By similarity		PRO_0000338352
	Chain	3300 – 3579	280	Non-structural protein 6 By similarity		PRO_0000338353
	Chain	3580 – 3662	83	Non-structural protein 7 By similarity		PRO_0000338354
	Chain	3663 – 3857	195	Non-structural protein 8 By similarity		PRO_0000338355
	Chain	3858 – 3965	108	Non-structural protein 9 By similarity		PRO_0000338356
	Chain	3966 – 4100	135	Non-structural protein 10 By similarity		PRO_0000338357
	Chain	4111 – 4117	7	Non-structural protein 11 By similarity		PRO_0000338358
Regions
	Transmembrane	1959 – 1979	21	Helical; Potential
	Transmembrane	2022 – 2042	21	Helical; Potential
	Transmembrane	2105 – 2125	21	Helical; Potential
	Transmembrane	2127 – 2147	21	Helical; Potential
	Transmembrane	2150 – 2170	21	Helical; Potential
	Transmembrane	2528 – 2548	21	Helical; Potential
	Transmembrane	2619 – 2639	21	Helical; Potential
	Transmembrane	2654 – 2674	21	Helical; Potential
	Transmembrane	2754 – 2774	21	Helical; Potential
	Transmembrane	2787 – 2807	21	Helical; Potential
	Transmembrane	2814 – 2834	21	Helical; Potential
	Transmembrane	2863 – 2883	21	Helical; Potential
	Transmembrane	3336 – 3356	21	Helical; Potential
	Transmembrane	3361 – 3381	21	Helical; Potential
	Transmembrane	3399 – 3419	21	Helical; Potential
	Transmembrane	3431 – 3451	21	Helical; Potential
	Transmembrane	3454 – 3474	21	Helical; Potential
	Transmembrane	3476 – 3496	21	Helical; Potential
	Transmembrane	3500 – 3520	21	Helical; Potential
	Domain	1057 – 1296	240	Peptidase C16 1
	Domain	1297 – 1465	169	Macro
	Domain	1691 – 1951	261	Peptidase C16 2
	Domain	2998 – 3299	302	Peptidase C30
	Zinc finger	1162 – 1193	32	C4-type
	Zinc finger	4039 – 4055	17	By similarity
	Zinc finger	4081 – 4094	14	By similarity
	Region	1959 – 2170	212	HD1
	Region	2528 – 2883	356	HD2
	Region	3336 – 3520	185	HD3
	Compositional bias	1816 – 1932	117	Val-rich
Sites
	Active site	1091	1	For PL1-PRO activity By similarity
	Active site	1239	1	For PL1-PRO activity By similarity
	Active site	1729	1	For PL2-PRO activity By similarity
	Active site	1888	1	For PL2-PRO activity By similarity
	Active site	3038	1	For 3CL-PRO activity By similarity
	Active site	3141	1	For 3CL-PRO activity By similarity
	Site	110 – 111	2	Cleavage; by PL1-PRO By similarity
	Site	895 – 896	2	Cleavage; by PL1-PRO By similarity
	Site	2516 – 2517	2	Cleavage; by PL2-PRO By similarity
	Site	2997 – 2998	2	Cleavage; by 3CL-PRO By similarity
	Site	3299 – 3300	2	Cleavage; by 3CL-PRO By similarity
	Site	3579 – 3580	2	Cleavage; by 3CL-PRO By similarity
	Site	3662 – 3663	2	Cleavage; by 3CL-PRO By similarity
	Site	3857 – 3858	2	Cleavage; by 3CL-PRO By similarity
	Site	3965 – 3966	2	Cleavage; by 3CL-PRO By similarity
	Site	4100 – 4101	2	Cleavage; by 3CL-PRO By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 4409589DAF0AA869	FASTA	4,117	452,818
	10 20 30 40 50 60 MASNHVTLAF ANDAEISAFG FCTASEAVSY YSEAAASGFM QCRFVSLDLA DTVEGLLPED 70 80 90 100 110 120 YVMVVIGTTK LSAYVDTFGS RPRNICGWLL FSNCNYFLEE LELTFGRRGG NIVPVDQYMC 130 140 150 160 170 180 GADGKPVLQE SEWEYTDFFA DSEDGQLNIA GITYVKAWIV ERSDVSYASQ NLTSIKSITY 190 200 210 220 230 240 CSTYEHTFLD GTAMKVARTP KIKKNVVLSE PLATIYREIG SPFVDNGSDA RSIIRRPVFL 250 260 270 280 290 300 HAFVKCKCGS YHWTVGDWTS YVSTCCGFKC KPVLVASCSA MPGSVVVTRA GAGTGVKYYN 310 320 330 340 350 360 NMFLRHVADI DGLAFWRILK VQSKDDLACS GKFLEHHEEG FTDPCYFLND SSLATKLKFD 370 380 390 400 410 420 ILSGKFSDEV KQAIIAGHVV VGSALVDIVD DALGQPWFIR KLGDLASAPW EQLKAVVRGL 430 440 450 460 470 480 GLLSDEVVLF GKRLSCATLS IVNGVFEFLA DVPEKLAAAV TVFVNFLNEF FESACDCLKV 490 500 510 520 530 540 GGKTFNKVGS YVLFDNALVK LVKAKARGPR QAGICEVRYT SLVVGSTTKV VSKRVENANV 550 560 570 580 590 600 NLVVVDEDVT LNTTGRTVVV DGLAFFESDG FYRHLADADV VIEHPVYKSA CELKPVFECD 610 620 630 640 650 660 PIPDFPLPVA ASVAELCVQT DLLLKNYNTP YKTYSCVVRG DKCCITCTLQ FKAPSYVEDA 670 680 690 700 710 720 VNFVDLCTKN IGTAGFHEFY ITAHEQQDLQ GFLTTCCTMS GFECFMPTIP QCPAVLEEID 730 740 750 760 770 780 GGSIWRSFIT GLNTMWDFCK RLKVSFGLDG IVVTVARKFK RLGALLAEMY NTYLSTVVEN 790 800 810 820 830 840 LVLAGVSFKY YATSVPKIVL GGCFHSVKSV FASVFQIPVQ AGIEKFKVFL NCVHPVVPRV 850 860 870 880 890 900 IETSFVELEE TTFKPPALNG GIAIVDGFAF YYDGTLYYPT DGNSVVPICF KKKGGGDVKF 910 920 930 940 950 960 SDEVSVKTID PVYKVSLEFE FESETIMAVL NKAVGNRIKV TGGWDDVVEY INVAIEVLKD 970 980 990 1000 1010 1020 HVEVPKYYIY DEEGGTDPNL PVMVSQWPLN DDTISQDLLD VEVVTDAPID SEGDEVDSSA 1030 1040 1050 1060 1070 1080 PEKVADVANS EPGDDGLPVA PETNVESEVE EVAATLSFIK DTPSTVTKDP FAFDFVSYGG 1090 1100 1110 1120 1130 1140 LKVLRQSHNN CWVTSTLVQL QLLGIVDDPA MELFSAGRVG PMVRKCYESQ KAILGSLGDV 1150 1160 1170 1180 1190 1200 SACLESLTKD LHTLKITCSV VCGCGTGERI YEGCAFRMTP TLEPFPYGAC AQCAQVLMHT 1210 1220 1230 1240 1250 1260 FKSIVGTGIF CRDTTALSLD SLVVKPLCAA AFIGKDSGHY VTNFYDAAMA IDGYGRHQIK 1270 1280 1290 1300 1310 1320 YDTLNTICVK DVNWTAPLVP AVDSVVEPVV KPFYSYKNVD FYQGDFSDLV KLPCDFVVNA 1330 1340 1350 1360 1370 1380 ANEKLSHGGG IAKAIDVYTK GMLQKCSNDY IKAHGPIKVG RGVMLEALGL KVFNVVGPRK 1390 1400 1410 1420 1430 1440 GKHAPELLVK AYKSVFANSG VALTPLISVG IFSVPLEESL SAFLACVGDR HCKCFCYGDK 1450 1460 1470 1480 1490 1500 EREAIIKYMD GLVDAIFKEA LVDTTPVQED VQQVSQKPVL PNFEPFRIEG AHAFYECNPE 1510 1520 1530 1540 1550 1560 GLMSLGADKL VLFTNSNLDF CSVGKCLNDV TSGALLEAIN VFKKSNKTVP AGNCVTLDCA 1570 1580 1590 1600 1610 1620 NMISITMVVL PFDGDANYDK NYARAVVKVS KLKGKLVLAV DDATLYSKLS HLSVLGFVST 1630 1640 1650 1660 1670 1680 PDDVERFYAN KSVVIKVTED TRSVKAVKVE STATYGQQIG PCLVNDTVVT DNKPVVADVV 1690 1700 1710 1720 1730 1740 AKVVPNANWD SHYGFDKAGE FHMLDHTGFT FPSEVVNGRR VIKTTDNNCW VNVTCLQLQF 1750 1760 1770 1780 1790 1800 ARFRFKSAGL QAMWESYCTG DVAMFVHWLY WLTGVDKGQP SDSENALNML SKYIVPAGSV 1810 1820 1830 1840 1850 1860 TIERVTHDGC CCSKRVVTAP VVNASVLKLG VEDGLCPHGL NYIGKVVVVK GTTIVVNVGK 1870 1880 1890 1900 1910 1920 PVVAPSHLFL KGVSYTTFLD NGNGVVGHYT VFDHGTGMVH DGDAFVPGDL NVSPVTNVVV 1930 1940 1950 1960 1970 1980 SEQTAVVIKD PVKKAELDAT KLLDTMNYAS ERFFSFGDFM SRNLITVFLY ILSILGLCFR 1990 2000 2010 2020 2030 2040 AFRKRDVKVL AGVPQRTGII LRKSMRYNAK ALGVFFKLKL YWFKVLGKFS LGIYALYALL 2050 2060 2070 2080 2090 2100 FMTIRFTPIG SPVCDDVVAG YANSSFDKNE YCNSVICKVC LYGYQELSDF SHTQVVWQHL 2110 2120 2130 2140 2150 2160 RDPLIGNVMP FFYLAFLAIF GGVYVKAITL YFIFQYLNSL GVFLGLQQSI WFLQLVPFDV 2170 2180 2190 2200 2210 2220 FGDEIVVFFI VTRVLMFIKH VCLGCDKASC VACSKSARLK RVPVQTIFQG TSKSFYVHAN 2230 2240 2250 2260 2270 2280 GGSKFCKKHN FFCLNCDSYG PGCTFINDVI ATEVGNVVKL NVQPTGPATI LIDKVEFSNG 2290 2300 2310 2320 2330 2340 FYYLYSGDTF WKYNFDITDS KYTCKEALKN CSIITDFIVF NNNGSNVNQV KNACVYFSQM 2350 2360 2370 2380 2390 2400 LCKPVKLVDS ALLASLSVDF GASLHSAFVS VLSNSFGKDL SSCNDMQDCK STLGFDDVPL 2410 2420 2430 2440 2450 2460 DTFNAAVAEA HRYDVLLTDM SFNNFTTSYA KPEEKFPVHD IATCMRVGAK IVNHNVLVKD 2470 2480 2490 2500 2510 2520 SIPVVWLVRD FIALSEETRK YIIRTTKVKG ITFMLTFNDC RMHTTIPTVC IANKKGAGLP 2530 2540 2550 2560 2570 2580 SFSKVKKFFW FLCLFIVAAF FALSFLDFST QVSSDSDYDF KYIESGQLKT FDNPLSCVHN 2590 2600 2610 2620 2630 2640 VFINFDQWHD AKFGFTPVNN PSCPIVVGVS DEARTVPGIP AGVYLAGKTL VFAINTIFGT 2650 2660 2670 2680 2690 2700 SGLCFDASGV ADKGACIFNS ACTTLSGLGG TAVYCYKNGL VEGAKLYSEL APHSYYKMVD 2710 2720 2730 2740 2750 2760 GNAVSLPEII SRGFGIRTIR TKAMTYCRVG QCVQSAEGVC FGADRFFVYN AESGSDFVCG 2770 2780 2790 2800 2810 2820 TGLFTLLMNV ISVFSKTVPV TVLSGQILFN CIIAFVAVAV CFLFTKFKRM FGDMSVGVFT 2830 2840 2850 2860 2870 2880 VGACTLLNNV SYIVTQNTLG MLGYATLYFL CTKGVRYMWI WHLGFLISYI LIAPWWVLMV 2890 2900 2910 2920 2930 2940 YAFSAIFEFM PNLFKLKVST QLFEGDKFVG SFENAAAGTF VLDMHAYERL ANSISTEKLR 2950 2960 2970 2980 2990 3000 QYASTYNKYK YYSGSASEAD YRLACFAHLA KAMMDYASNH NDTLYTPPTV SYNSTLQAGL 3010 3020 3030 3040 3050 3060 RKMAQPSGVV EKCIVRVCYG NMALNGLWLG DIVMCPRHVI ASSTTSTIDY DYALSVLRLH 3070 3080 3090 3100 3110 3120 NFSISSGNVF LGVVSATMRG ALLQIKVNQN NVHTPKYTYR TVRPGESFNI LACYDGAAAG 3130 3140 3150 3160 3170 3180 VYGVNMRSNY TIRGSFINGA CGSPGYNINN GTVEFCYLHQ LELGSGCHVG SDLDGVMYGG 3190 3200 3210 3220 3230 3240 YEDQPTLQVE GASSLFTENV LAFLYAALIN GSTWWLSSSR IAVDRFNEWA VHNGMTTVGN 3250 3260 3270 3280 3290 3300 TDCFSILAAK TGVDVQRLLA SIQSLHKNFG GKQILGHTSL TDEFTTGEVV RQMYGVNLQG 3310 3320 3330 3340 3350 3360 GYVSRACRNV LLVGSFLTFF WSELVSYTKF FWVNPGYVTP MFACLSLLSS LLMFTLKHKT 3370 3380 3390 3400 3410 3420 LFFQVFLIPA LIVTSCINLA FDVEVYNYLA EHFDYHVSLM GFNAQGLVNI FVCFVVTILH 3430 3440 3450 3460 3470 3480 GTYTWRFFNT PASSVTYVVA LLTAAYNYFY ASDILSCAMT LFASVTGNWF VGAVCYKVAV 3490 3500 3510 3520 3530 3540 YMALRFPTFV AIFGDIKSVM FCYLVLGYFT CCFYGILYWF NRFFKVSVGV YDYTVSAAEF 3550 3560 3570 3580 3590 3600 KYMVANGLRA PTGTLDSLLL SAKLIGIGGE RNIKISSVQS KLTDIKCSNV VLLGCLSSMN 3610 3620 3630 3640 3650 3660 VSANSTEWAY CVDLHNKINL CNDPEKAQEM LLALLAFFLS KNSAFGLDDL LESYFNDNSM 3670 3680 3690 3700 3710 3720 LQSVASTYVG LPSYVIYENA RQQYEDAVNN GSPPQLVKQL RHAMNVAKSE FDREASTQRK 3730 3740 3750 3760 3770 3780 LDRMAEQAAA QMYKEARAVN RKSKVVSAMH SLLFGMLRRL DMSSVDTILN LAKDGVVPLS 3790 3800 3810 3820 3830 3840 VIPAVSATKL NIVTSDIDSY NRIQREGCVH YAGTIWNIID IKDNDGKVVH VKEVTAQNAE 3850 3860 3870 3880 3890 3900 SLSWPLVLGC ERIVKLQNNE IIPGKLKQRS IKAEGDGIVG EGKALYNNEG GRTFMYAFIS 3910 3920 3930 3940 3950 3960 DKPDLRVVKW EFDGGCNTIE LEPPRKFLVD SPNGAQIKYL YFVRNLNTLR RGAVLGYIGA 3970 3980 3990 4000 4010 4020 TVRLQAGKQT EQAINSSLLT LCAFAVDPAK TYIDAVKSGH KPVGNCVKML ANGSGNGQAV 4030 4040 4050 4060 4070 4080 TNGVEASTNQ DSYGGASVCL YCRAHVEHPS MDGFCRLKGK YVQVPLGTVD PIRFVLENDV 4090 4100 4110 CKVCGCWLSN GCTCDRSIMQ STDMAYLNEY GALVQLD
	Isoform Replicase polyprotein 1ab (pp1ab) [UniParc]. See P0C6Y4.		–	–

References

[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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF353511 Genomic RNA. No translation available.
3D structure databases
ProteinModelPortal	P0C6V6.
SMR	P0C6V6. Positions 2998-3297, 3860-3964, 3972-4096.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002589. A1pp. 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]
Pfam	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]
SMART	SM00506. A1pp. 1 hit. [Graphical view]
SUPFAM	SSF101816. Nsp9. 1 hit. SSF51126. Pectin_lyas_like. 1 hit. SSF50494. Pept_Ser_Cys. 1 hit. SSF144246. SSF144246. 1 hit.
PROSITE	PS51442. M_PRO. 1 hit. PS51154. MACRO. 1 hit. PS51124. PEPTIDASE_C16. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

R1A_PEDV7

Accession

Primary (citable) accession number: P0C6V6
Secondary accession number(s): Q91AV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	May 29, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program