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P0C6V0 (R1A_CVMA5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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):
    p28
  2. Non-structural protein 2
    Short name=nsp2
    Alternative name(s):
    p65
  3. Non-structural protein 3
    Short name=nsp3
    EC=3.4.19.12
    EC=3.4.22.69
    Alternative name(s):
    PL1-PRO/PL2-PRO
    PL1/PL2
    Papain-like proteinases 1/2
    p210
  4. Non-structural protein 4
    Short name=nsp4
    Alternative name(s):
    Peptide HD2
    p44
  5. 3C-like proteinase
    Short name=3CL-PRO
    Short name=3CLp
    EC=3.4.22.-
    Alternative name(s):
    M-PRO
    nsp5
    p27
  6. Non-structural protein 6
    Short name=nsp6
  7. Non-structural protein 7
    Short name=nsp7
    Alternative name(s):
    p10
  8. Non-structural protein 8
    Short name=nsp8
    Alternative name(s):
    p22
  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
    p15
  11. Non-structural protein 11
    Short name=nsp11
Gene names
ORF Names:1a
OrganismMurine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus) [Reference proteome]
Taxonomic identifier11142 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length4468 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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.

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.

Catalytic activity

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).

Subunit structure

3CL-PRO exists as monomer and homodimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer By similarity.

Subcellular location

Non-structural protein 3: Host membrane; Multi-pass membrane protein Potential.

Non-structural protein 4: Host membrane; Multi-pass membrane protein Potential.

Non-structural protein 6: Host membrane; Multi-pass membrane protein Potential.

Non-structural protein 7: Host 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.

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.

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.

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.

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 processActivation of host autophagy by virus
Decay of host mRNAs by virus
Host gene expression shutoff by virus
Host mRNA suppression by virus
Host translation shutoff 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
   Cellular componentHost cytoplasm
Host membrane
Membrane
   Coding sequence diversityRibosomal frameshifting
   DomainRepeat
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinduction by virus of catabolism of host mRNA

Inferred from electronic annotation. Source: UniProtKB-KW

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 ISG15 activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host translation

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host type I interferon-mediated signaling pathway

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_componenthost cell membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionRNA 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: P0C6V0-1)

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: P0C6X9-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 44684468Replicase polyprotein 1a
PRO_0000338278
Chain1 – 247247Non-structural protein 1 Probable
PRO_0000338279
Chain248 – 832585Non-structural protein 2 Probable
PRO_0000338280
Chain833 – 28372005Non-structural protein 3 Probable
PRO_0000338281
Chain2838 – 3333496Non-structural protein 4
PRO_0000338282
Chain3334 – 36353023C-like proteinase
PRO_0000338283
Chain3636 – 3921286Non-structural protein 6 Probable
PRO_0000338284
Chain3922 – 401392Non-structural protein 7
PRO_0000338285
Chain4014 – 4207194Non-structural protein 8
PRO_0000338286
Chain4208 – 4317110Non-structural protein 9
PRO_0000338287
Chain4318 – 4454137Non-structural protein 10
PRO_0000338288
Chain4455 – 446814Non-structural protein 11 Potential
PRO_0000338289

Regions

Transmembrane2286 – 230621Helical; Potential
Transmembrane2314 – 233421Helical; Potential
Transmembrane2400 – 242021Helical; Potential
Transmembrane2442 – 246221Helical; Potential
Transmembrane2625 – 264521Helical; Potential
Transmembrane2847 – 286721Helical; Potential
Transmembrane3096 – 311621Helical; Potential
Transmembrane3118 – 313821Helical; Potential
Transmembrane3150 – 317021Helical; Potential
Transmembrane3177 – 319721Helical; Potential
Transmembrane3202 – 322221Helical; Potential
Transmembrane3644 – 366421Helical; Potential
Transmembrane3674 – 369421Helical; Potential
Transmembrane3699 – 371921Helical; Potential
Transmembrane3742 – 376221Helical; Potential
Transmembrane3769 – 378921Helical; Potential
Transmembrane3796 – 381621Helical; Potential
Transmembrane3840 – 386021Helical; Potential
Domain1084 – 1333250Peptidase C16 1
Domain1323 – 1482160Macro
Domain1678 – 1937260Peptidase C16 2
Domain3334 – 3635302Peptidase C30
Zinc finger1198 – 122629C4-type 1
Zinc finger1794 – 183037C4-type 2
Zinc finger4391 – 440717 By similarity
Zinc finger4433 – 444614 By similarity
Region2225 – 2645421HD1
Region2847 – 3222376HD2
Region3526 – 3860335HD3

Sites

Active site11211For PL1-PRO activity By similarity
Active site12721For PL1-PRO activity By similarity
Active site17161For PL2-PRO activity By similarity
Active site18731For PL2-PRO activity By similarity
Active site33741For 3CL-PRO activity By similarity
Active site34781For 3CL-PRO activity
Site247 – 2482Cleavage; by PL1-PRO Probable
Site832 – 8332Cleavage; by PL1-PRO Probable
Site2837 – 28382Cleavage; by PL2-PRO
Site3333 – 33342Cleavage; by 3CL-PRO
Site3635 – 36362Cleavage; by 3CL-PRO
Site3921 – 39222Cleavage; by 3CL-PRO
Site4013 – 40142Cleavage; by 3CL-PRO
Site4207 – 42082Cleavage; by 3CL-PRO
Site4317 – 43182Cleavage; by 3CL-PRO
Site4454 – 44552Cleavage; by 3CL-PRO

Natural variations

Natural variant16991P → S in strain: Isolate C12 mutant.
Natural variant21961M → K in strain: Isolate C12 mutant.

Experimental info

Mutagenesis33311F → A, H or W: No effect. Ref.5
Mutagenesis33321L → I or S: No processing between peptide HD2 and 3CL-PRO. Ref.5
Mutagenesis33331Q → A, K or R: No processing between peptide HD2 and 3CL-PRO. Ref.5
Mutagenesis33341S → A: No effect. Ref.5
Mutagenesis33341S → C: No processing between peptide HD2 and 3CL-PRO. Ref.5
Mutagenesis33351G → A: No effect. Ref.5
Mutagenesis33351G → P: No processing between peptide HD2 and 3CL-PRO. Ref.5
Mutagenesis33361I → L: No effect. Ref.5
Mutagenesis34781C → A: Complete loss of 3CL-PRO activity. Ref.5
Sequence conflict287 – 2882WR → CA Ref.3
Sequence conflict3111L → V Ref.3
Sequence conflict5701D → G Ref.3
Sequence conflict36201E → EL Ref.2
Sequence conflict37111T → TL Ref.2
Sequence conflict39681M → V Ref.2

Secondary structure

.................... 4468
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 53FB55E845B646A5

FASTA4,468496,341
        10         20         30         40         50         60 
MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK GKTLVNHVRV 

        70         80         90        100        110        120 
NCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG SAVLVKPSKR LSIQAWTNLG 

       130        140        150        160        170        180 
VLPKTAAMGL FKRVCLCNTR ECSCDAHVAF HLFTVQPDGV CLGNGRFIGW FVPVTAIPEY 

       190        200        210        220        230        240 
AKQWLQPWSI LLRKGGNKGS VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSCKAYA 

       250        260        270        280        290        300 
LLKGYRGVKP ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELFPVWRDS LDSEVLVAWH 

       310        320        330        340        350        360 
VDRDPRAAMR LQTLATVRCI DYVGQPTEDV VDGDVVVREP AHLLAANAIV KRLPRLVETM 

       370        380        390        400        410        420 
LYTDSSVTEF CYKTKLCECG FITQFGYVDC CGDTCDFRGW VAGNMMDGFP CPGCTKNYMP 

       430        440        450        460        470        480 
WELEAQSSGV IPEGGVLFTQ STDTVNRESF KLYGHAVVPF GSAVYWSPCP GMWLPVIWSS 

       490        500        510        520        530        540 
VKSYSGLTYT GVVGCKAIVQ ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN 

       550        560        570        580        590        600 
RGDYSLLLEN VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN 

       610        620        630        640        650        660 
FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT EWFDLAVDIA 

       670        680        690        700        710        720 
ASAAGWLCYQ LVNGLFAVAN GVITFVQEVP ELVKNFVDKF KAFFKVLIDS MSVSILSGLT 

       730        740        750        760        770        780 
VVKTASNRVC LAGSKVYEVV QKSLSAYVMP VGCSEATCLV GEIEPAVFED DVVDVVKAPL 

       790        800        810        820        830        840 
TYQGCCKPPT SFEKICIVDK LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVEFND 

       850        860        870        880        890        900 
KPKVRKIPST RKIKITFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC 

       910        920        930        940        950        960 
KEHDVIGTKV CALLDRLAGD YVYLFDEGGD EVIAPRMYCS FSAPDDEDCV AADVVDADEN 

       970        980        990       1000       1010       1020 
QDDDAEDSAV LVADTQEEDG VAKGQVEADS EICVAHTGSQ EELAEPDAVG SQTPIASAEE 

      1030       1040       1050       1060       1070       1080 
TEVGEASDRE GIAEAKATVC ADAVDACPDQ VEAFEIEKVE DSILDELQTE LNAPADKTYE 

      1090       1100       1110       1120       1130       1140 
DVLAFDAVCS EALSAFYAVP SDETHFKVCG FYSPAIERTN CWLRSTLIVM QSLPLEFKDL 

      1150       1160       1170       1180       1190       1200 
EMQKLWLSYK AGYDQCFVDK LVKSVPKSII LPQGGYVADF AYFFLSQCSF KAYANWRCLE 

      1210       1220       1230       1240       1250       1260 
CDMELKLQGL DAMFFYGDVV SHMCKCGNSM TLLSADIPYT LHFGVRDDKF CAFYTPRKVF 

      1270       1280       1290       1300       1310       1320 
RAACAVDVND CHSMAVVEGK QIDGKVVTKF IGDKFDFMVG YGMTFSMSPF ELAQLYGSCI 

      1330       1340       1350       1360       1370       1380 
TPNVCFVKGD VIKVVRLVNA EVIVNPANGR MAHGAGVAGA IAEKAGSAFI KETSDMVKAQ 

      1390       1400       1410       1420       1430       1440 
GVCQVGECYE SAGGKLCKKV LNIVGPDARG HGKQCYSLLE RAYQHINKCD NVVTTLISAG 

      1450       1460       1470       1480       1490       1500 
IFSVPTDVSL TYLLGVVTKN VILVSNNQDD FDVIEKCQVT SVAGTKALSL QLAKNLCRDV 

      1510       1520       1530       1540       1550       1560 
KFVTNACSSL FSESCFVSSY DVLQEVEALR HDIQLDDDAR VFVQANMDCL PTDWRLVNKF 

      1570       1580       1590       1600       1610       1620 
DSVDGVRTIK YFECPGGIFV SSQGKKFGYV QNGSFKEASV SQIRALLANK VDVLCTVDGV 

      1630       1640       1650       1660       1670       1680 
NFRSCCVAEG EVFGKTLGSV FCDGINVTKV RCSAIYKGKV FFQYSDLSEA DLVAVKDAFG 

      1690       1700       1710       1720       1730       1740 
FDEPQLLKYY TMLGMCKWPV VVCGNYFAFK QSNNNCYINV ACLMLQHLSL KFPKWQWQEA 

      1750       1760       1770       1780       1790       1800 
WNEFRSGKPL RFVSLVLAKG SFKFNEPSDS IDFMRVVLRE ADLSGATCNL EFVCKCGVKQ 

      1810       1820       1830       1840       1850       1860 
EQRKGVDAVM HFGTLDKGDL VRGYNIACTC GSKLVHCTQF NVPFLICSNT PEGRKLPDDV 

      1870       1880       1890       1900       1910       1920 
VAANIFTGGS VGHYTHVKCK PKYQLYDACN VNKVSEAKGN FTDCLYLKNL KQTFSSVLTT 

      1930       1940       1950       1960       1970       1980 
FYLDDVKCVE YKPDLSQYYC ESGKYYTKPI IKAQFRTFEK VDGVYTNFKL VGHSIAEKLN 

      1990       2000       2010       2020       2030       2040 
AKLGFDCNSP FVEYKITEWP TATGDVVLAS DDLYVSRYSS GCITFGKPVV WLGHEEASLK 

      2050       2060       2070       2080       2090       2100 
SLTYFNRPSV VCENKFNVLP VDVSEPTDKG PVPAAVLVTG VPGADASAGA GIAKEQKACA 

      2110       2120       2130       2140       2150       2160 
SASVEDQVVT EVRQEPSVSA ADVKEVKLNG VKKPVKVEGS VVVNDPTSET KVVKSLSIVD 

      2170       2180       2190       2200       2210       2220 
VYDMFLTGCK YVVWTANELS RLVNSPTVRE YVKWGMGKIV TPAKLLLLRD EKQEFVAPKV 

      2230       2240       2250       2260       2270       2280 
VKAKAIACYC AVKWFLLYCF SWIKFNTDNK VIYTTEVASK LTFKLCCLAF KNALQTFNWS 

      2290       2300       2310       2320       2330       2340 
VVSRGFFLVA TVFLLWFNFL YANVILSDFY LPNIGPLPTF VGQIVAWFKT TFGVSTICDF 

      2350       2360       2370       2380       2390       2400 
YQVTDLGYRS SFCNGSMVCE LCFSGFDMLD NYDAINVVQH VVDRRLSFDY ISLFKLVVEL 

      2410       2420       2430       2440       2450       2460 
VIGYSLYTVC FYPLFVLIGM QLLTTWLPEF FMLETMHWSA RLFVFVANML PAFTLLRFYI 

      2470       2480       2490       2500       2510       2520 
VVTAMYKVYC LCRHVMYGCS KPGCLFCYKR NRSVRVKCST VVGGSLRYYD VMANGGTGFC 

      2530       2540       2550       2560       2570       2580 
TKHQWNCLNC NSWKPGNTFI THEAAADLSK ELKRPVNPTD SAYYSVTEVK QVGCSMRLFY 

      2590       2600       2610       2620       2630       2640 
ERDGQRVYDD VNASLFVDMN GLLHSKVKGV PETHVVVVEN EADKAGFLGA AVFYAQSLYR 

      2650       2660       2670       2680       2690       2700 
PMLMVEKKLI TTANTGLSVS RTMFDLYVDS LLNVLDVDRK SLTSFVNAAH NSLKEGVQLE 

      2710       2720       2730       2740       2750       2760 
QVMDTFIGCA RRKCAIDSDV ETKSITKSVM SAVNAGVDFT DESCNNLVPT YVKSDTIVAA 

      2770       2780       2790       2800       2810       2820 
DLGVLIQNNA KHVQANVAKA ANVACIWSVD AFNQLSADLQ HRLRKACSKT GLKIKLTYNK 

      2830       2840       2850       2860       2870       2880 
QEANVPILTT PFSLKGGAVF SRMLQWLFVA NLICFIVLWA LMPTYAVHKS DMQLPLYASF 

      2890       2900       2910       2920       2930       2940 
KVIDNGVLRD VSVTDACFAN KFNQFDQWYE STFGLAYYRN SKACPVVVAV IDQDIGHTLF 

      2950       2960       2970       2980       2990       3000 
NVPTTVLRYG FHVLHFITHA FATDSVQCYT PHMQIPYDNF YASGCVLSSL CTMLAHADGT 

      3010       3020       3030       3040       3050       3060 
PHPYCYTGGV MHNASLYSSL APHVRYNLAS SNGYIRFPEV VSEGIVRVVR TRSMTYCRVG 

      3070       3080       3090       3100       3110       3120 
LCEEAEEGIC FNFNRSWVLN NPYYRAMPGT FCGRNAFDLI HQVLGGLVRP IDFFALTASS 

      3130       3140       3150       3160       3170       3180 
VAGAILAIIV VLAFYYLIKL KRAFGDYTSV VVINVIVWCI NFLMLFVFQV YPTLSCLYAC 

      3190       3200       3210       3220       3230       3240 
FYFYTTLYFP SEISVVMHLQ WLVMYGAIMP LWFCIIYVAV VVSNHALWLF SYCRKIGTEV 

      3250       3260       3270       3280       3290       3300 
RSDGTFEEMA LTTFMITKES YCKLKNSVSD VAFNRYLSLY NKYRYFSGKM DTAAYREAAC 

      3310       3320       3330       3340       3350       3360 
SQLAKAMETF NHNNGNDVLY QPPTASVTTS FLQSGIVKMV SPTSKVEPCI VSVTYGNMTL 

      3370       3380       3390       3400       3410       3420 
NGLWLDDKVY CPRHVICSSA DMTDPDYPNL LCRVTSSDFC VMSGRMSLTV MSYQMQGCQL 

      3430       3440       3450       3460       3470       3480 
VLTVTLQNPN TPKYSFGVVK PGETFTVLAA YNGRPQGAFH VTLRSSHTIK GSFLCGSCGS 

      3490       3500       3510       3520       3530       3540 
VGYVLTGDSV RFVYMHQLEL STGCHTGTDF SGNFYGPYRD AQVVQLPVQD YTQTVNVVAW 

      3550       3560       3570       3580       3590       3600 
LYAAIFNRCN WFVQSDSCSL EEFNVWAMTN GFSSIKADLV LDALASMTGV TVEQVLAAIK 

      3610       3620       3630       3640       3650       3660 
RLHSGFQGKQ ILGSCVLEDE TPSDVYQQLA GVKLQSKRTR VIKGTCCWIL ASTFLFCSII 

      3670       3680       3690       3700       3710       3720 
SAFVKWTMFM YVTTHMLGVT LCALCFVSFA MLLIKHKHLY LTMYIMPVLC TFYTNYLVVY 

      3730       3740       3750       3760       3770       3780 
KQSFRGLAYA WLSHFVPAVD YTYMDEVLYG VVLLVAMVFV TMRSINHDVF SIMFLVGRLV 

      3790       3800       3810       3820       3830       3840 
SLVSMWYFGA NLEEEVLLFL TSLFGTYTWT TMLSLATAKV IAKWLAVNVL YFTDVPQIKL 

      3850       3860       3870       3880       3890       3900 
VLLSYLCIGY VCCCYWGILS LLNSIFRMPL GVYNYKISVQ ELRYMNANGL RPPRNSFEAL 

      3910       3920       3930       3940       3950       3960 
MLNFKLLGIG GVPVIEVSQI QSRLTDVKCA NVVLLNCLQH LHIASNSKLW QYCSTLHNEI 

      3970       3980       3990       4000       4010       4020 
LATSDLSMAF DKLAQLLVVL FANPAAVDSK CLASIEEVSD DYVRDNTVLQ ALQSEFVNMA 

      4030       4040       4050       4060       4070       4080 
SFVEYELAKK NLDEAKASGS ANQQQIKQLE KACNIAKSAY ERDRAVARKL ERMADLALTN 

      4090       4100       4110       4120       4130       4140 
MYKEARINDK KSKVVSALQT MLFSMVRKLD NQALNSILDN AVKGCVPLNA IPSLTSNTLT 

      4150       4160       4170       4180       4190       4200 
IIVPDKQVFD QVVDNVYVTY AGNVWHIQFI QDADGAVKQL NEIDVNSTWP LVIAANRHNE 

      4210       4220       4230       4240       4250       4260 
VSTVVLQNNE LMPQKLRTQV VNSGSDMNCN TPTQCYYNTT GTGKIVYAIL SDCDGLKYTK 

      4270       4280       4290       4300       4310       4320 
IVKEDGNCVV LELDPPCKFS VQDVKGLKIK YLYFVKGCNT LARGWVVGTL SSTVRLQAGT 

      4330       4340       4350       4360       4370       4380 
ATEYASNSAI LSLCAFSVDP KKTYLDYIKQ GGVPVTNCVK MLCDHAGTGM AITIKPEATT 

      4390       4400       4410       4420       4430       4440 
NQDSYGGASV CIYCRSRVEH PDVDGLCKLR GKFVQVPLGI KDPVSYVLTH DVCQVCGFWR 

      4450       4460 
DGSCSCVGTG SQFQSKDTNF LNGFGVQV 

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Isoform Replicase polyprotein 1ab (pp1ab) [UniParc].

See P0C6X9.

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73559 Genomic RNA. No translation available.
AF029248 Genomic RNA. Translation: AAB86820.1.
M27198 Genomic RNA. Translation: AAA74011.1.
PIRA32440.
S15760.
RefSeqNP_045298.1. NC_001846.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M0ANMR-A833-946[»]
ProteinModelPortalP0C6V0.
SMRP0C6V0. Positions 4049-4199, 4323-4447.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1489749.

Family and domain databases

InterProIPR022570. Coronavirus_NSP1.
IPR002589. Macro_dom.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR002705. Pept_C30/C16_sub.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view]
PfamPF11963. 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]
SMARTSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEPS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameR1A_CVMA5
AccessionPrimary (citable) accession number: P0C6V0
Secondary accession number(s): P16342
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: April 16, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references