Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0C6V0

- R1A_CVMA5

UniProt

P0C6V0 - R1A_CVMA5

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) 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. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent 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
Non-structural protein 1: binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (By similarity).By similarity

Catalytic activityi

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.
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
Sitei247 – 2482Cleavage; by PL1-PROCurated
Sitei832 – 8332Cleavage; by PL1-PROCurated
Active sitei1121 – 11211For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1272 – 12721For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1716 – 17161For PL2-PRO activityPROSITE-ProRule annotation
Active sitei1873 – 18731For PL2-PRO activityPROSITE-ProRule annotation
Sitei2837 – 28382Cleavage; by PL2-PRO
Sitei3333 – 33342Cleavage; by 3CL-PRO
Active sitei3374 – 33741For 3CL-PRO activityPROSITE-ProRule annotation
Active sitei3478 – 34781For 3CL-PRO activity
Sitei3635 – 36362Cleavage; by 3CL-PRO
Sitei3921 – 39222Cleavage; by 3CL-PRO
Sitei4013 – 40142Cleavage; by 3CL-PRO
Sitei4207 – 42082Cleavage; by 3CL-PRO
Sitei4317 – 43182Cleavage; by 3CL-PRO
Sitei4454 – 44552Cleavage; by 3CL-PRO

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1198 – 122629C4-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1794 – 183037C4-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4391 – 440717By similarityAdd
BLAST
Zinc fingeri4433 – 444614By 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 catabolism of host mRNA Source: UniProtKB-KW
  2. induction by virus of host autophagy Source: UniProtKB-KW
  3. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
  4. suppression by virus of host IRF3 activity Source: UniProtKB-KW
  5. suppression by virus of host ISG15 activity Source: UniProtKB-KW
  6. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
  7. viral genome replication Source: InterPro
  8. viral protein processing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Activation of host autophagy by virus, Decay of host mRNAs by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host IRF3 by virus, Inhibition of host ISG15 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):
p28
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p65
Alternative name(s):
PL1-PRO/PL2-PRO
PL1/PL2
Papain-like proteinases 1/2
p210
Non-structural protein 4
Short name:
nsp4
Alternative name(s):
Peptide HD2
p44
3C-like proteinase (EC:3.4.22.-)
Short name:
3CL-PRO
Short name:
3CLp
Alternative name(s):
M-PRO
nsp5
p27
Non-structural protein 6
Short name:
nsp6
Non-structural protein 7
Short name:
nsp7
Alternative name(s):
p10
Non-structural protein 8
Short name:
nsp8
Alternative name(s):
p22
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
p15
Non-structural protein 11
Short name:
nsp11
Gene namesi
ORF Names:1a
OrganismiMurine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus)
Taxonomic identifieri11142 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000007192: 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.
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.
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.
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2286 – 230621HelicalSequence AnalysisAdd
BLAST
Transmembranei2314 – 233421HelicalSequence AnalysisAdd
BLAST
Transmembranei2400 – 242021HelicalSequence AnalysisAdd
BLAST
Transmembranei2442 – 246221HelicalSequence AnalysisAdd
BLAST
Transmembranei2625 – 264521HelicalSequence AnalysisAdd
BLAST
Transmembranei2847 – 286721HelicalSequence AnalysisAdd
BLAST
Transmembranei3096 – 311621HelicalSequence AnalysisAdd
BLAST
Transmembranei3118 – 313821HelicalSequence AnalysisAdd
BLAST
Transmembranei3150 – 317021HelicalSequence AnalysisAdd
BLAST
Transmembranei3177 – 319721HelicalSequence AnalysisAdd
BLAST
Transmembranei3202 – 322221HelicalSequence AnalysisAdd
BLAST
Transmembranei3644 – 366421HelicalSequence AnalysisAdd
BLAST
Transmembranei3674 – 369421HelicalSequence AnalysisAdd
BLAST
Transmembranei3699 – 371921HelicalSequence AnalysisAdd
BLAST
Transmembranei3742 – 376221HelicalSequence AnalysisAdd
BLAST
Transmembranei3769 – 378921HelicalSequence AnalysisAdd
BLAST
Transmembranei3796 – 381621HelicalSequence AnalysisAdd
BLAST
Transmembranei3840 – 386021HelicalSequence AnalysisAdd
BLAST

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3331 – 33311F → A, H or W: No effect. 1 Publication
Mutagenesisi3332 – 33321L → I or S: No processing between peptide HD2 and 3CL-PRO. 1 Publication
Mutagenesisi3333 – 33331Q → A, K or R: No processing between peptide HD2 and 3CL-PRO. 1 Publication
Mutagenesisi3334 – 33341S → A: No effect. 1 Publication
Mutagenesisi3334 – 33341S → C: No processing between peptide HD2 and 3CL-PRO. 1 Publication
Mutagenesisi3335 – 33351G → A: No effect. 1 Publication
Mutagenesisi3335 – 33351G → P: No processing between peptide HD2 and 3CL-PRO. 1 Publication
Mutagenesisi3336 – 33361I → L: No effect. 1 Publication
Mutagenesisi3478 – 34781C → A: Complete loss of 3CL-PRO activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 44684468Replicase polyprotein 1aPRO_0000338278Add
BLAST
Chaini1 – 247247Non-structural protein 1CuratedPRO_0000338279Add
BLAST
Chaini248 – 832585Non-structural protein 2CuratedPRO_0000338280Add
BLAST
Chaini833 – 28372005Non-structural protein 3CuratedPRO_0000338281Add
BLAST
Chaini2838 – 3333496Non-structural protein 4PRO_0000338282Add
BLAST
Chaini3334 – 36353023C-like proteinasePRO_0000338283Add
BLAST
Chaini3636 – 3921286Non-structural protein 6CuratedPRO_0000338284Add
BLAST
Chaini3922 – 401392Non-structural protein 7PRO_0000338285Add
BLAST
Chaini4014 – 4207194Non-structural protein 8PRO_0000338286Add
BLAST
Chaini4208 – 4317110Non-structural protein 9PRO_0000338287Add
BLAST
Chaini4318 – 4454137Non-structural protein 10PRO_0000338288Add
BLAST
Chaini4455 – 446814Non-structural protein 11Sequence AnalysisPRO_0000338289Add
BLAST

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. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer (By similarity).By similarity

Structurei

Secondary structure

1
4468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi840 – 8423Combined sources
Beta strandi849 – 8535Combined sources
Beta strandi859 – 8613Combined sources
Helixi862 – 8709Combined sources
Beta strandi874 – 8774Combined sources
Helixi882 – 89615Combined sources
Helixi904 – 9074Combined sources
Helixi909 – 91810Combined sources
Beta strandi923 – 9308Combined sources
Beta strandi935 – 9428Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M0ANMR-A833-946[»]
ProteinModelPortaliP0C6V0.
SMRiP0C6V0. Positions 4049-4199, 4323-4447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1084 – 1333250Peptidase C16 1PROSITE-ProRule annotationAdd
BLAST
Domaini1323 – 1482160MacroPROSITE-ProRule annotationAdd
BLAST
Domaini1678 – 1937260Peptidase C16 2PROSITE-ProRule annotationAdd
BLAST
Domaini3334 – 3635302Peptidase C30PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2225 – 2645421HD1Add
BLAST
Regioni2847 – 3222376HD2Add
BLAST
Regioni3526 – 3860335HD3Add
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 fingeri1198 – 122629C4-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1794 – 183037C4-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4391 – 440717By similarityAdd
BLAST
Zinc fingeri4433 – 444614By similarityAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

InterProiIPR022570. Coronavirus_NSP1.
IPR002589. Macro_dom.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR002705. Pept_C30/C16_B_coronavir.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases-like.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF11963. DUF3477. 2 hits.
PF01661. Macro. 1 hit.
PF09401. NSP10. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF01831. Peptidase_C16. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMiSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF53335. SSF53335. 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: P0C6V0-1) [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

        10         20         30         40         50
MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK
60 70 80 90 100
GKTLVNHVRV NCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG
110 120 130 140 150
SAVLVKPSKR LSIQAWTNLG VLPKTAAMGL FKRVCLCNTR ECSCDAHVAF
160 170 180 190 200
HLFTVQPDGV CLGNGRFIGW FVPVTAIPEY AKQWLQPWSI LLRKGGNKGS
210 220 230 240 250
VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSCKAYA LLKGYRGVKP
260 270 280 290 300
ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELFPVWRDS LDSEVLVAWH
310 320 330 340 350
VDRDPRAAMR LQTLATVRCI DYVGQPTEDV VDGDVVVREP AHLLAANAIV
360 370 380 390 400
KRLPRLVETM LYTDSSVTEF CYKTKLCECG FITQFGYVDC CGDTCDFRGW
410 420 430 440 450
VAGNMMDGFP CPGCTKNYMP WELEAQSSGV IPEGGVLFTQ STDTVNRESF
460 470 480 490 500
KLYGHAVVPF GSAVYWSPCP GMWLPVIWSS VKSYSGLTYT GVVGCKAIVQ
510 520 530 540 550
ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN RGDYSLLLEN
560 570 580 590 600
VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN
610 620 630 640 650
FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT
660 670 680 690 700
EWFDLAVDIA ASAAGWLCYQ LVNGLFAVAN GVITFVQEVP ELVKNFVDKF
710 720 730 740 750
KAFFKVLIDS MSVSILSGLT VVKTASNRVC LAGSKVYEVV QKSLSAYVMP
760 770 780 790 800
VGCSEATCLV GEIEPAVFED DVVDVVKAPL TYQGCCKPPT SFEKICIVDK
810 820 830 840 850
LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVEFND KPKVRKIPST
860 870 880 890 900
RKIKITFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC
910 920 930 940 950
KEHDVIGTKV CALLDRLAGD YVYLFDEGGD EVIAPRMYCS FSAPDDEDCV
960 970 980 990 1000
AADVVDADEN QDDDAEDSAV LVADTQEEDG VAKGQVEADS EICVAHTGSQ
1010 1020 1030 1040 1050
EELAEPDAVG SQTPIASAEE TEVGEASDRE GIAEAKATVC ADAVDACPDQ
1060 1070 1080 1090 1100
VEAFEIEKVE DSILDELQTE LNAPADKTYE DVLAFDAVCS EALSAFYAVP
1110 1120 1130 1140 1150
SDETHFKVCG FYSPAIERTN CWLRSTLIVM QSLPLEFKDL EMQKLWLSYK
1160 1170 1180 1190 1200
AGYDQCFVDK LVKSVPKSII LPQGGYVADF AYFFLSQCSF KAYANWRCLE
1210 1220 1230 1240 1250
CDMELKLQGL DAMFFYGDVV SHMCKCGNSM TLLSADIPYT LHFGVRDDKF
1260 1270 1280 1290 1300
CAFYTPRKVF RAACAVDVND CHSMAVVEGK QIDGKVVTKF IGDKFDFMVG
1310 1320 1330 1340 1350
YGMTFSMSPF ELAQLYGSCI TPNVCFVKGD VIKVVRLVNA EVIVNPANGR
1360 1370 1380 1390 1400
MAHGAGVAGA IAEKAGSAFI KETSDMVKAQ GVCQVGECYE SAGGKLCKKV
1410 1420 1430 1440 1450
LNIVGPDARG HGKQCYSLLE RAYQHINKCD NVVTTLISAG IFSVPTDVSL
1460 1470 1480 1490 1500
TYLLGVVTKN VILVSNNQDD FDVIEKCQVT SVAGTKALSL QLAKNLCRDV
1510 1520 1530 1540 1550
KFVTNACSSL FSESCFVSSY DVLQEVEALR HDIQLDDDAR VFVQANMDCL
1560 1570 1580 1590 1600
PTDWRLVNKF DSVDGVRTIK YFECPGGIFV SSQGKKFGYV QNGSFKEASV
1610 1620 1630 1640 1650
SQIRALLANK VDVLCTVDGV NFRSCCVAEG EVFGKTLGSV FCDGINVTKV
1660 1670 1680 1690 1700
RCSAIYKGKV FFQYSDLSEA DLVAVKDAFG FDEPQLLKYY TMLGMCKWPV
1710 1720 1730 1740 1750
VVCGNYFAFK QSNNNCYINV ACLMLQHLSL KFPKWQWQEA WNEFRSGKPL
1760 1770 1780 1790 1800
RFVSLVLAKG SFKFNEPSDS IDFMRVVLRE ADLSGATCNL EFVCKCGVKQ
1810 1820 1830 1840 1850
EQRKGVDAVM HFGTLDKGDL VRGYNIACTC GSKLVHCTQF NVPFLICSNT
1860 1870 1880 1890 1900
PEGRKLPDDV VAANIFTGGS VGHYTHVKCK PKYQLYDACN VNKVSEAKGN
1910 1920 1930 1940 1950
FTDCLYLKNL KQTFSSVLTT FYLDDVKCVE YKPDLSQYYC ESGKYYTKPI
1960 1970 1980 1990 2000
IKAQFRTFEK VDGVYTNFKL VGHSIAEKLN AKLGFDCNSP FVEYKITEWP
2010 2020 2030 2040 2050
TATGDVVLAS DDLYVSRYSS GCITFGKPVV WLGHEEASLK SLTYFNRPSV
2060 2070 2080 2090 2100
VCENKFNVLP VDVSEPTDKG PVPAAVLVTG VPGADASAGA GIAKEQKACA
2110 2120 2130 2140 2150
SASVEDQVVT EVRQEPSVSA ADVKEVKLNG VKKPVKVEGS VVVNDPTSET
2160 2170 2180 2190 2200
KVVKSLSIVD VYDMFLTGCK YVVWTANELS RLVNSPTVRE YVKWGMGKIV
2210 2220 2230 2240 2250
TPAKLLLLRD EKQEFVAPKV VKAKAIACYC AVKWFLLYCF SWIKFNTDNK
2260 2270 2280 2290 2300
VIYTTEVASK LTFKLCCLAF KNALQTFNWS VVSRGFFLVA TVFLLWFNFL
2310 2320 2330 2340 2350
YANVILSDFY LPNIGPLPTF VGQIVAWFKT TFGVSTICDF YQVTDLGYRS
2360 2370 2380 2390 2400
SFCNGSMVCE LCFSGFDMLD NYDAINVVQH VVDRRLSFDY ISLFKLVVEL
2410 2420 2430 2440 2450
VIGYSLYTVC FYPLFVLIGM QLLTTWLPEF FMLETMHWSA RLFVFVANML
2460 2470 2480 2490 2500
PAFTLLRFYI VVTAMYKVYC LCRHVMYGCS KPGCLFCYKR NRSVRVKCST
2510 2520 2530 2540 2550
VVGGSLRYYD VMANGGTGFC TKHQWNCLNC NSWKPGNTFI THEAAADLSK
2560 2570 2580 2590 2600
ELKRPVNPTD SAYYSVTEVK QVGCSMRLFY ERDGQRVYDD VNASLFVDMN
2610 2620 2630 2640 2650
GLLHSKVKGV PETHVVVVEN EADKAGFLGA AVFYAQSLYR PMLMVEKKLI
2660 2670 2680 2690 2700
TTANTGLSVS RTMFDLYVDS LLNVLDVDRK SLTSFVNAAH NSLKEGVQLE
2710 2720 2730 2740 2750
QVMDTFIGCA RRKCAIDSDV ETKSITKSVM SAVNAGVDFT DESCNNLVPT
2760 2770 2780 2790 2800
YVKSDTIVAA DLGVLIQNNA KHVQANVAKA ANVACIWSVD AFNQLSADLQ
2810 2820 2830 2840 2850
HRLRKACSKT GLKIKLTYNK QEANVPILTT PFSLKGGAVF SRMLQWLFVA
2860 2870 2880 2890 2900
NLICFIVLWA LMPTYAVHKS DMQLPLYASF KVIDNGVLRD VSVTDACFAN
2910 2920 2930 2940 2950
KFNQFDQWYE STFGLAYYRN SKACPVVVAV IDQDIGHTLF NVPTTVLRYG
2960 2970 2980 2990 3000
FHVLHFITHA FATDSVQCYT PHMQIPYDNF YASGCVLSSL CTMLAHADGT
3010 3020 3030 3040 3050
PHPYCYTGGV MHNASLYSSL APHVRYNLAS SNGYIRFPEV VSEGIVRVVR
3060 3070 3080 3090 3100
TRSMTYCRVG LCEEAEEGIC FNFNRSWVLN NPYYRAMPGT FCGRNAFDLI
3110 3120 3130 3140 3150
HQVLGGLVRP IDFFALTASS VAGAILAIIV VLAFYYLIKL KRAFGDYTSV
3160 3170 3180 3190 3200
VVINVIVWCI NFLMLFVFQV YPTLSCLYAC FYFYTTLYFP SEISVVMHLQ
3210 3220 3230 3240 3250
WLVMYGAIMP LWFCIIYVAV VVSNHALWLF SYCRKIGTEV RSDGTFEEMA
3260 3270 3280 3290 3300
LTTFMITKES YCKLKNSVSD VAFNRYLSLY NKYRYFSGKM DTAAYREAAC
3310 3320 3330 3340 3350
SQLAKAMETF NHNNGNDVLY QPPTASVTTS FLQSGIVKMV SPTSKVEPCI
3360 3370 3380 3390 3400
VSVTYGNMTL NGLWLDDKVY CPRHVICSSA DMTDPDYPNL LCRVTSSDFC
3410 3420 3430 3440 3450
VMSGRMSLTV MSYQMQGCQL VLTVTLQNPN TPKYSFGVVK PGETFTVLAA
3460 3470 3480 3490 3500
YNGRPQGAFH VTLRSSHTIK GSFLCGSCGS VGYVLTGDSV RFVYMHQLEL
3510 3520 3530 3540 3550
STGCHTGTDF SGNFYGPYRD AQVVQLPVQD YTQTVNVVAW LYAAIFNRCN
3560 3570 3580 3590 3600
WFVQSDSCSL EEFNVWAMTN GFSSIKADLV LDALASMTGV TVEQVLAAIK
3610 3620 3630 3640 3650
RLHSGFQGKQ ILGSCVLEDE TPSDVYQQLA GVKLQSKRTR VIKGTCCWIL
3660 3670 3680 3690 3700
ASTFLFCSII SAFVKWTMFM YVTTHMLGVT LCALCFVSFA MLLIKHKHLY
3710 3720 3730 3740 3750
LTMYIMPVLC TFYTNYLVVY KQSFRGLAYA WLSHFVPAVD YTYMDEVLYG
3760 3770 3780 3790 3800
VVLLVAMVFV TMRSINHDVF SIMFLVGRLV SLVSMWYFGA NLEEEVLLFL
3810 3820 3830 3840 3850
TSLFGTYTWT TMLSLATAKV IAKWLAVNVL YFTDVPQIKL VLLSYLCIGY
3860 3870 3880 3890 3900
VCCCYWGILS LLNSIFRMPL GVYNYKISVQ ELRYMNANGL RPPRNSFEAL
3910 3920 3930 3940 3950
MLNFKLLGIG GVPVIEVSQI QSRLTDVKCA NVVLLNCLQH LHIASNSKLW
3960 3970 3980 3990 4000
QYCSTLHNEI LATSDLSMAF DKLAQLLVVL FANPAAVDSK CLASIEEVSD
4010 4020 4030 4040 4050
DYVRDNTVLQ ALQSEFVNMA SFVEYELAKK NLDEAKASGS ANQQQIKQLE
4060 4070 4080 4090 4100
KACNIAKSAY ERDRAVARKL ERMADLALTN MYKEARINDK KSKVVSALQT
4110 4120 4130 4140 4150
MLFSMVRKLD NQALNSILDN AVKGCVPLNA IPSLTSNTLT IIVPDKQVFD
4160 4170 4180 4190 4200
QVVDNVYVTY AGNVWHIQFI QDADGAVKQL NEIDVNSTWP LVIAANRHNE
4210 4220 4230 4240 4250
VSTVVLQNNE LMPQKLRTQV VNSGSDMNCN TPTQCYYNTT GTGKIVYAIL
4260 4270 4280 4290 4300
SDCDGLKYTK IVKEDGNCVV LELDPPCKFS VQDVKGLKIK YLYFVKGCNT
4310 4320 4330 4340 4350
LARGWVVGTL SSTVRLQAGT ATEYASNSAI LSLCAFSVDP KKTYLDYIKQ
4360 4370 4380 4390 4400
GGVPVTNCVK MLCDHAGTGM AITIKPEATT NQDSYGGASV CIYCRSRVEH
4410 4420 4430 4440 4450
PDVDGLCKLR GKFVQVPLGI KDPVSYVLTH DVCQVCGFWR DGSCSCVGTG
4460
SQFQSKDTNF LNGFGVQV

Note: Produced by conventional translation.

Length:4,468
Mass (Da):496,341
Last modified:June 10, 2008 - v1
Checksum:i53FB55E845B646A5
GO
Isoform Replicase polyprotein 1ab (identifier: P0C6X9-1) [UniParc]FASTAAdd to Basket

Also known as: pp1ab

The sequence of this isoform can be found in the external entry P0C6X9.
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:7,176
Mass (Da):802,596
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2882WR → CA(PubMed:2545027)Curated
Sequence conflicti311 – 3111L → V(PubMed:2545027)Curated
Sequence conflicti570 – 5701D → G(PubMed:2545027)Curated
Sequence conflicti3620 – 36201E → EL(PubMed:9426441)Curated
Sequence conflicti3711 – 37111T → TL(PubMed:9426441)Curated
Sequence conflicti3968 – 39681M → V(PubMed:9426441)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1699 – 16991P → S in strain: Isolate C12 mutant.
Natural varianti2196 – 21961M → K in strain: Isolate C12 mutant.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73559 Genomic RNA. No translation available.
AF029248 Genomic RNA. Translation: AAB86820.1.
M27198 Genomic RNA. Translation: AAA74011.1.
PIRiA32440.
S15760.
RefSeqiNP_045298.1. NC_001846.1.

Genome annotation databases

GeneIDi1489749.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73559 Genomic RNA. No translation available.
AF029248 Genomic RNA. Translation: AAB86820.1 .
M27198 Genomic RNA. Translation: AAA74011.1 .
PIRi A32440.
S15760.
RefSeqi NP_045298.1. NC_001846.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2M0A NMR - A 833-946 [» ]
ProteinModelPortali P0C6V0.
SMRi P0C6V0. Positions 4049-4199, 4323-4447.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1489749.

Family and domain databases

InterProi IPR022570. Coronavirus_NSP1.
IPR002589. Macro_dom.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR002705. Pept_C30/C16_B_coronavir.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases-like.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view ]
Pfami PF11963. DUF3477. 2 hits.
PF01661. Macro. 1 hit.
PF09401. NSP10. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF01831. Peptidase_C16. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view ]
SMARTi SM00506. A1pp. 1 hit.
[Graphical view ]
SUPFAMi SSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEi PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: heterogeneity among MHV strains."
    Bonilla P.J., Gorbalenya A.E., Weiss S.R.
    Virology 198:736-740(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is associated with a Q159L amino acid substitution in the spike protein."
    Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.
    Virology 239:1-10(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate C12 mutant.
  3. "Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59."
    Pachuk C.J., Bredenbeek P.J., Zoltick P.W., Spaan W.J.M., Weiss S.R.
    Virology 171:141-148(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-597.
  4. "Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro."
    Lu X.T., Sims A.C., Denison M.R.
    J. Virol. 72:2265-2271(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, CHARACTERIZATION OF NSP8.
  5. "Further requirements for cleavage by the murine coronavirus 3C-like proteinase: identification of a cleavage site within ORF1b."
    Pinon J.D., Teng H., Weiss S.R.
    Virology 263:471-484(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF PHE-3331; LEU-3332; GLN-3333; SER-3334; GLY-3335; ILE-3336 AND CYS-3478.
  6. "Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly."
    Bost A.G., Carnahan R.H., Lu X.T., Denison M.R.
    J. Virol. 74:3379-3387(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, CHARACTERIZATION OF NSP7; NSP9 AND NSP10.

Entry informationi

Entry nameiR1A_CVMA5
AccessioniPrimary (citable) accession number: P0C6V0
Secondary accession number(s): P16342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: November 26, 2014
This is version 51 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, Reference 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