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P19811 (RPOA_EAVBU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 133. 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 1ab
Alternative name(s):
ORF1ab polyprotein

Cleaved into the following 14 chains:

  1. Nsp1 papain-like cysteine proteinase
    Short name=PCP
    EC=3.4.22.-
  2. Nsp2 cysteine proteinase
    EC=3.4.19.12
    EC=3.4.22.-
    Alternative name(s):
    CP2
    Short name=CP
  3. Non-structural protein 3
    Short name=Nsp3
  4. 3C-like serine proteinase
    Short name=3CLSP
    EC=3.4.21.-
    Alternative name(s):
    Nsp4
  5. Non-structural protein 5-6-7
    Short name=Nsp5-6-7
  6. Non-structural protein 5
    Short name=Nsp5
  7. Non-structural protein 6
    Short name=Nsp6
  8. Non-structural protein 7-alpha
    Short name=Nsp7-alpha
  9. Non-structural protein 7-beta
    Short name=Nsp7-beta
  10. Non-structural protein 8
    Short name=Nsp8
  11. RNA-directed RNA polymerase
    Short name=Pol
    Short name=RdRp
    EC=2.7.7.48
    Alternative name(s):
    Nsp9
  12. Helicase
    Short name=Hel
    EC=3.6.4.12
    EC=3.6.4.13
    Alternative name(s):
    Nsp10
  13. Non-structural protein 11
    Short name=Nsp11
  14. Non-structural protein 12
    Short name=Nsp12
Gene names
Name:rep
ORF Names:1a-1b
OrganismEquine arteritis virus (strain Bucyrus) (EAV) [Reference proteome]
Taxonomic identifier299386 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageNidoviralesArteriviridaeArterivirus
Virus hostEquidae (horses) [TaxID: 9788]

Protein attributes

Sequence length3175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. Ref.15

Nsp1 is essential for viral subgenomic mRNA synthesis. Ref.15

Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity. Ref.15

The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein. Ref.15

The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Ref.15

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

ATP + H2O = ADP + phosphate.

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

Nsp1 interacts with cellular transcription cofactor SND1/p100. Ref.14

Subcellular location

Nsp1 papain-like cysteine proteinase: Host nucleus. Host cytoplasm Ref.9 Ref.13.

Nsp2 cysteine proteinase: Host membrane; Multi-pass membrane protein Potential Ref.9 Ref.13.

Non-structural protein 3: Host membrane; Multi-pass membrane protein Potential Ref.9 Ref.13.

Non-structural protein 5-6-7: Host membrane; Multi-pass membrane protein Potential Ref.9 Ref.13.

3C-like serine proteinase: Host cytoplasm Potential Ref.9 Ref.13.

RNA-directed RNA polymerase: Host cytoplasmhost perinuclear region Potential Ref.9 Ref.13.

Helicase: Host cytoplasmhost perinuclear region Potential Ref.9 Ref.13.

Domain

The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.

The OTU-like region is responsible for the deubiquitinating and deISGylation activities of Nsp2 Probable.

Post-translational modification

Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. There are two alternative pathways for processing. Either nsp4-5 is cleaved, which represents the major pathway or the nsp5-6 and nsp6-7 are processed, which represents the minor pathway. The major pathway occurs when nsp2 acts as cofactor for nsp4. Ref.4 Ref.6 Ref.8 Ref.10 Ref.16

Miscellaneous

Nsp1 contains an inactivated papain-like cysteine proteinase domain due to a Lys instead of a Cys in position 73.

Sequence similarities

Belongs to the arteriviridae polyprotein family.

Contains 1 (+)RNA virus helicase ATP-binding domain.

Contains 1 (+)RNA virus helicase C-terminal domain.

Contains 1 AV MBD (arterivirus metal-binding) domain.

Contains 1 peptidase C31 domain.

Contains 1 peptidase C32 domain.

Contains 1 peptidase C33 domain.

Contains 1 peptidase S32 domain.

Contains 1 RdRp catalytic domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Inhibition of host innate immune response by virus
Inhibition of host interferon signaling pathway by virus
Inhibition of host ISG15 by virus
Modulation of host ubiquitin pathway by viral deubiquitinase
Modulation of host ubiquitin pathway by virus
Viral immunoevasion
Viral RNA replication
   Cellular componentHost cytoplasm
Host membrane
Host nucleus
Membrane
   Coding sequence diversityRibosomal frameshifting
   DomainTransmembrane
Transmembrane helix
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHelicase
Hydrolase
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Serine protease
Thiol protease
Transferase
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processmodulation by virus of host protein ubiquitination

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 type I interferon-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral RNA 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 nucleus

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_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type exopeptidase activity

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 1ab (identifier: P19811-1)

Also known as: pp1ab;

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 -1 ribosomal frameshifting at the 1a-1b genes boundary.
Isoform Replicase polyprotein 1a (identifier: P19811-2)

Also known as: pp1a; ORF1a polyprotein;

The sequence of this isoform differs from the canonical sequence as follows:
     1728-3175: Missing.
Note: Produced by conventional translation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 31753175Replicase polyprotein 1ab
PRO_0000036619
Chain1 – 260260Nsp1 papain-like cysteine proteinase
PRO_0000036621
Chain261 – 831571Nsp2 cysteine proteinase
PRO_0000036622
Chain832 – 1064233Non-structural protein 3
PRO_0000036623
Chain1065 – 12682043C-like serine proteinase
PRO_0000036624
Chain1269 – 1677409Non-structural protein 5-6-7
PRO_0000036625
Chain1269 – 1430162Non-structural protein 5
PRO_0000423106
Chain1431 – 145222Non-structural protein 6
PRO_0000423107
Chain1453 – 1575123Non-structural protein 7-alpha
PRO_0000423108
Chain1576 – 1677102Non-structural protein 7-beta
PRO_0000423109
Chain1678 – 2370693RNA-directed RNA polymerase
PRO_0000036626
Chain1678 – 172750Non-structural protein 8
PRO_0000036627
Chain2371 – 2837467Helicase
PRO_0000036628
Chain2838 – 3056219Non-structural protein 11
PRO_0000036629
Chain3057 – 3175119Non-structural protein 12
PRO_0000036630

Regions

Transmembrane530 – 55021Helical; Potential
Transmembrane551 – 57121Helical; Potential
Transmembrane625 – 64521Helical; Potential
Transmembrane829 – 84921Helical; Potential
Transmembrane903 – 92321Helical; Potential
Transmembrane935 – 95521Helical; Potential
Transmembrane977 – 99721Helical; Potential
Transmembrane1291 – 131121Helical; Potential
Transmembrane1333 – 135321Helical; Potential
Transmembrane1355 – 137521Helical; Potential
Transmembrane1385 – 140521Helical; Potential
Domain66 – 15691Peptidase C31
Domain157 – 260104Peptidase C32
Domain261 – 360100Peptidase C33
Domain1065 – 1268204Peptidase S32
Domain2116 – 2251136RdRp catalytic
Domain2371 – 243868AV MBD
Domain2496 – 2661166(+)RNA virus helicase ATP-binding
Domain2662 – 2793132(+)RNA virus helicase C-terminal
Zinc finger25 – 4420C4-type; atypical
Nucleotide binding2528 – 25358ATP By similarity
Region261 – 33979OTU-like
Region530 – 645116HD1
Region829 – 997169HD2
Region1291 – 1405115HD3
Compositional bias389 – 44052Pro-rich

Sites

Active site1641For Nsp1 papain-like cysteine proteinase activity
Active site2301For Nsp1 papain-like cysteine proteinase activity
Active site2701For Nsp2 cysteine proteinase activity
Active site3321For Nsp2 cysteine proteinase activity
Active site11031Charge relay system; for 3C-like serine proteinase activity By similarity
Active site11291Charge relay system; for 3C-like serine proteinase activity By similarity
Active site11841Charge relay system; for 3C-like serine proteinase activity By similarity
Site260 – 2612Cleavage; by PCP
Site831 – 8322Cleavage; by Nsp2 cysteine proteinase
Site1064 – 10652Cleavage; by 3CLSP
Site1268 – 12692Cleavage; by 3CLSP; in major pathway
Site1430 – 14312Cleavage; by 3CLSP; in minor pathway
Site1452 – 14532Cleavage; by 3CLSP; in minor pathway
Site1575 – 15762Cleavage; by 3CLSP
Site1677 – 16782Cleavage; by 3CLSP
Site2370 – 23712Cleavage; by 3CLSP
Site24291Involved in mRNA transcription process
Site2837 – 28382Cleavage; by 3CLSP
Site3056 – 30572Cleavage; by 3CLSP

Amino acid modifications

Glycosylation15011N-linked (GlcNAc...); by host Probable

Natural variations

Alternative sequence1728 – 31751448Missing in isoform Replicase polyprotein 1a.
VSP_032887

Experimental info

Mutagenesis251C → A: Complete loss of transcription. Ref.12
Mutagenesis441C → A: Complete loss of transcription. Ref.12
Mutagenesis1641C → G or S: Complete loss of PCP proteinase activity. Ref.4 Ref.6
Mutagenesis2191H → A, G or V: No effect. Ref.4
Mutagenesis2301H → A, G or V: Complete loss of PCP proteinase activity. Ref.4
Mutagenesis2601G → V: Complete loss of nsp1-nsp2 cleavage. Ref.4
Mutagenesis2701C → A, H, R or S: Complete loss of CP2 activity. Ref.5
Mutagenesis2711G → W: Complete loss of CP2 activity. Ref.5
Mutagenesis2911D → E or N: No effect. Ref.5
Mutagenesis2951D → E or N: No effect. Ref.5
Mutagenesis2961D → E or N: No effect. Ref.5
Mutagenesis2971E → D or Q: No effect. Ref.5
Mutagenesis3191C → A, H or P: Complete loss of CP2 activity. Ref.5
Mutagenesis3321H → C, I, N or Y: Complete loss of CP2 activity. Ref.5
Mutagenesis3441C → A: No effect. Ref.5
Mutagenesis3441C → H: Almost complete loss of CP2 activity. Ref.5
Mutagenesis3491C → A, H or S: Complete loss of CP2 activity. Ref.5
Mutagenesis3541C → A, H or P: Complete loss of CP2 activity. Ref.5
Mutagenesis3561C → A: Complete loss of CP2 activity. Ref.5
Mutagenesis3561C → H: No effect. Ref.5
Mutagenesis8311G → P: Complete loss of nsp2-nsp3 cleavage. Ref.6
Mutagenesis10641E → P: Complete loss of nsp3-nsp4 cleavage. Ref.6
Mutagenesis11031H → G or R: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. Ref.6
Mutagenesis11171D → N or T: No effect. Ref.6
Mutagenesis11291D → E: Complete loss of nsp3-nsp4 and nsp5-nsp6 cleavages. Ref.6
Mutagenesis11291D → K or V: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. Ref.6
Mutagenesis11791T → G or S: Partial loss of nsp4-nsp5 cleavage. Ref.6
Mutagenesis11791T → N: Increased nsp5-nsp6 cleavage. Ref.6
Mutagenesis11841S → C, F, I or T: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. Ref.6
Mutagenesis11981H → L, R or Y: Complete loss of nsp4-nsp5 and nsp5-nsp6 cleavages. Ref.6
Mutagenesis12681E → P: Complete loss of nsp3-nsp4 and nsp4-nsp5 cleavages. Ref.6 Ref.8
Mutagenesis14301E → P: No effect. Ref.6
Mutagenesis16771E → P: Complete loss of nsp5-nsp6 cleavage. Ref.6
Mutagenesis23511D → P: No effect. Ref.10
Mutagenesis23701E → P: Complete loss of nsp9-nsp10 cleavage. Ref.10
Mutagenesis24291S → P: RNA can replicate efficiently but does not produce the subgenomic mRNAs required for structural protein expression. Ref.7
Mutagenesis28001E → P: No effect. Ref.10
Mutagenesis28191D → P: No effect. Ref.10
Mutagenesis28351E → D, P or Q: Almost complete loss of nsp9-nsp10 cleavage. Ref.10
Mutagenesis28371Q → D or N: No effect. Ref.10
Mutagenesis28371Q → E: Increased nsp9-nsp10 cleavage. Ref.10
Mutagenesis28371Q → P: Almost complete loss of nsp9-nsp10 cleavage. Ref.10
Mutagenesis30561E → P: Complete loss of nsp10-nsp11 cleavage. Ref.10

Secondary structure

......................................................................................................................................................... 3175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Replicase polyprotein 1ab (pp1ab) [UniParc].

Last modified April 13, 2004. Version 3.
Checksum: CB536C1F5091045C

FASTA3,175345,384
        10         20         30         40         50         60 
MATFSATGFG GSFVRDWSLD LPDACEHGAG LCCEVDGSTL CAECFRGCEG MEQCPGLFMG 

        70         80         90        100        110        120 
LLKLASPVPV GHKFLIGWYR AAKVTGRYNF LELLQHPAFA QLRVVDARLA IEEASVFIST 

       130        140        150        160        170        180 
DHASAKRFPG ARFALTPVYA NAWVVSPAAN SLIVTTDQEQ DGFCWLKLLP PDRREAGLRL 

       190        200        210        220        230        240 
YYNHYREQRT GWLSKTGLRL WLGDLGLGIN ASSGGLKFHI MRGSPQRAWH ITTRSCKLKS 

       250        260        270        280        290        300 
YYVCDISEAD WSCLPAGNYG GYNPPGDGAC GYRCLAFMNG ATVVSAGCSS DLWCDDELAY 

       310        320        330        340        350        360 
RVFQLSPTFT VTIPGGRVCP NAKYAMICDK QHWRVKRAKG VGLCLDESCF RGICNCQRMS 

       370        380        390        400        410        420 
GPPPAPVSAA VLDHILEAAT FGNVRVVTPE GQPRPVPAPR VRPSANSSGD VKDPAPVPPV 

       430        440        450        460        470        480 
PKPRTKLATP NPTQAPIPAP RTRLQGASTQ EPLASAGVAS DSAPKWRVAK TVYSSAERFR 

       490        500        510        520        530        540 
TELVQRARSV GDVLVQALPL KTPAVQRYTM TLKMMRSRFS WHCDVWYPLA VIACLLPIWP 

       550        560        570        580        590        600 
SLALLLSFAI GLIPSVGNNV VLTALLVSSA NYVASMDHQC EGAACLALLE EEHYYRAVRW 

       610        620        630        640        650        660 
RPITGALSLV LNLLGQVGYV ARSTFDAAYV PCTVFDLCSF AILYLCRNRC WRCFGRCVRV 

       670        680        690        700        710        720 
GPATHVLGST GQRVSKLALI DLCDHFSKPT IDVVGMATGW SGCYTGTAAM ERQCASTVDP 

       730        740        750        760        770        780 
HSFDQKKAGA TVYLTPPVNS GSALQCLNVM WKRPIGSTVL GEQTGAVVTA VKSISFSPPC 

       790        800        810        820        830        840 
CVSTTLPTRP GVTVVDHALY NRLTASGVDP ALLRVGQGDF LKLNPGFRLI GGWIYGICYF 

       850        860        870        880        890        900 
VLVVVSTFTC LPIKCGIGTR DPFCRRVFSV PVTKTQEHCH AGMCASAEGI SLDSLGLTQL 

       910        920        930        940        950        960 
QSYWIAAVTS GLVILLVCHR LAISALDLLT LASPLVLLVF PWASVGLLLA CSLAGAAVKI 

       970        980        990       1000       1010       1020 
QLLATLFVNL FFPQATLVTM GYWACVAALA VYSLMGLRVK VNVPMCVTPA HFLLLARSAG 

      1030       1040       1050       1060       1070       1080 
QSREQMLRVS AAAPTNSLLG VARDCYVTGT TRLYIPKEGG MVFEGLFRSP KARGNVGFVA 

      1090       1100       1110       1120       1130       1140 
GSSYGTGSVW TRNNEVVVLT ASHVVGRANM ATLKIGDAML TLTFKKNGDF AEAVTTQSEL 

      1150       1160       1170       1180       1190       1200 
PGNWPQLHFA QPTTGPASWC TATGDEEGLL SGEVCLAWTT SGDSGSAVVQ GDAVVGVHTG 

      1210       1220       1230       1240       1250       1260 
SNTSGVAYVT TPSGKLLGAD TVTLSSLSKH FTGPLTSIPK DIPDNIIADV DAVPRSLAML 

      1270       1280       1290       1300       1310       1320 
IDGLSNRESS LSGPQLLLIA CFMWSYLNQP AYLPYVLGFF AANFFLPKSV GRPVVTGLLW 

      1330       1340       1350       1360       1370       1380 
LCCLFTPLSM RLCLFHLVCA TVTGNVISLW FYITAAGTSY LSEMWFGGYP TMLFVPRFLV 

      1390       1400       1410       1420       1430       1440 
YQFPGWAIGT VLAVCSITML AAALGHTLLL DVFSASGRFD RTFMMKYFLE GGVKESVTAS 

      1450       1460       1470       1480       1490       1500 
VTRAYGKPIT QESLTATLAA LTDDDFQFLS DVLDCRAVRS AMNLRAALTS FQVAQYRNIL 

      1510       1520       1530       1540       1550       1560 
NASLQVDRDA ARSRRLMAKL ADFAVEQEVT AGDRVVVIDG LDRMAHFKDD LVLVPLTTKV 

      1570       1580       1590       1600       1610       1620 
VGGSRCTICD VVKEEANDTP VKPMPSRRRR KGLPKGAQLE WDRHQEEKRN AGDDDFAVSN 

      1630       1640       1650       1660       1670       1680 
DYVKRVPKYW DPSDTRGTTV KIAGTTYQKV VDYSGNVHYV EHQEDLLDYV LGKGSYEGLD 

      1690       1700       1710       1720       1730       1740 
QDKVLDLTNM LKVDPTELSS KDKAKARQLA HLLLDLANPV EAVNQLNLRA PHIFPGDVGR 

      1750       1760       1770       1780       1790       1800 
RTFADSKDKG FVALHSRTMF LAARDFLFNI KFVCDEEFTK TPKDTLLGYV RACPGYWFIF 

      1810       1820       1830       1840       1850       1860 
RRTHRSLIDA YWDSMECVYA LPTISDFDVS PGDVAVTGER WDFESPGGGR AKRLTADLVH 

      1870       1880       1890       1900       1910       1920 
AFQGFHGASY SYDDKVAAAV SGDPYRSDGV LYNTRWGNIP YSVPTNALEA TACYRAGCEA 

      1930       1940       1950       1960       1970       1980 
VTDGTNVIAT IGPFPEQQPI PDIPKSVLDN CADISCDAFI APAAETALCG DLEKYNLSTQ 

      1990       2000       2010       2020       2030       2040 
GFVLPSVFSM VRAYLKEEIG DAPPLYLPST VPSKNSQAGI NGAEFPTKSL QSYCLIDDMV 

      2050       2060       2070       2080       2090       2100 
SQSMKSNLQT ATMATCKRQY CSKYKIRSIL GTNNYIGLGL RACLSGVTAA FQKAGKDGSP 

      2110       2120       2130       2140       2150       2160 
IYLGKSKFDP IPAPDKYCLE TDLESCDRST PALVRWFATN LIFELAGQPE LVHSYVLNCC 

      2170       2180       2190       2200       2210       2220 
HDLVVAGSVA FTKRGGLSSG DPITSISNTI YSLVLYTQHM LLCGLEGYFP EIAEKYLDGS 

      2230       2240       2250       2260       2270       2280 
LELRDMFKYV RVYIYSDDVV LTTPNQHYAA SFDRWVPHLQ ALLGFKVDPK KTVNTSSPSF 

      2290       2300       2310       2320       2330       2340 
LGCRFKQVDG KCYLASLQDR VTRSLLYHIG AKNPSEYYEA AVSIFKDSII CCDEDWWTDL 

      2350       2360       2370       2380       2390       2400 
HRRISGAART DGVEFPTIEM LTSFRTKQYE SAVCTVCGAA PVAKSACGGW FCGNCVPYHA 

      2410       2420       2430       2440       2450       2460 
GHCHTTSLFA NCGHDIMYRS TYCTMCEGSP KQMVPKVPHP ILDHLLCHID YGSKEELTLV 

      2470       2480       2490       2500       2510       2520 
VADGRTTSPP GRYKVGHKVV AVVADVGGNI VFGCGPGSHI AVPLQDTLKG VVVNKALKNA 

      2530       2540       2550       2560       2570       2580 
AASEYVEGPP GSGKTFHLVK DVLAVVGSAT LVVPTHASML DCINKLKQAG ADPYFVVPKY 

      2590       2600       2610       2620       2630       2640 
TVLDFPRPGS GNITVRLPQV GTSEGETFVD EVAYFSPVDL ARILTQGRVK GYGDLNQLGC 

      2650       2660       2670       2680       2690       2700 
VGPASVPRNL WLRHFVSLEP LRVCHRFGAA VCDLIKGIYP YYEPAPHTTK VVFVPNPDFE 

      2710       2720       2730       2740       2750       2760 
KGVVITAYHK DRGLGHRTID SIQGCTFPVV TLRLPTPQSL TRPRAVVAVT RASQELYIYD 

      2770       2780       2790       2800       2810       2820 
PFDQLSGLLK FTKEAEAQDL IHGPPTACHL GQEIDLWSNE GLEYYKEVNL LYTHVPIKDG 

      2830       2840       2850       2860       2870       2880 
VIHSYPNCGP ACGWEKQSNK ISCLPRVAQN LGYHYSPDLP GFCPIPKELA EHWPVVSNDR 

      2890       2900       2910       2920       2930       2940 
YPNCLQITLQ QVCELSKPCS AGYMVGQSVF VQTPGVTSYW LTEWVDGKAR ALPDSLFSSG 

      2950       2960       2970       2980       2990       3000 
RFETNSRAFL DEAEEKFAAA HPHACLGEIN KSTVGGSHFI FSQYLPPLLP ADAVALVGAS 

      3010       3020       3030       3040       3050       3060 
LAGKAAKAAC SVVDVYAPSF EPYLHPETLS RVYKIMIDFK PCRLMVWRNA TFYVQEGVDA 

      3070       3080       3090       3100       3110       3120 
VTSALAAVSK LIKVPANEPV SFHVASGYRT NALVAPQAKI SIGAYAAEWA LSTEPPPAGY 

      3130       3140       3150       3160       3170 
AIVRRYIVKR LLSSTEVFLC RRGVVSSTSV QTICALEGCK PLFNFLQIGS VIGPV 

« Hide

Isoform Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [UniParc].

Checksum: FB0DB046FA0C74F6
Show »

FASTA1,727186,992

References

[1]"Equine arteritis virus is not a togavirus but belongs to the coronaviruslike superfamily."
den Boon J.A., Snijder E.J., Chirnside E.D., de Vries A.A.F., Horzinek M.C., Spaan W.J.M.
J. Virol. 65:2910-2920(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]Snijder E.J.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"All subgenomic mRNAs of equine arteritis virus contain a common leader sequence."
de Vries A.A.F., Chirnside E.D., Bredenbeek P.J., Gravestein L.A., Horzinek M.C., Spaan W.J.M.
Nucleic Acids Res. 18:3241-3247(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-17.
[4]"The 5' end of the equine arteritis virus replicase gene encodes a papainlike cysteine protease."
Snijder E.J., Wassenaar A.L.M., Spaan W.J.M.
J. Virol. 66:7040-7048(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, CHARACTERIZATION OF PCP, MUTAGENESIS OF CYS-164; HIS-219; HIS-230 AND GLY-260.
[5]"The arterivirus Nsp2 protease. An unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases."
Snijder E.J., Wassenaar A.L.M., Spaan W.J.M., Gorbalenya A.E.
J. Biol. Chem. 270:16671-16676(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF NSP2, MUTAGENESIS OF CYS-270; GLY-271; ASP-291; ASP-295; ASP-296; GLU-297; CYS-319; HIS-332; CYS-344; CYS-349; CYS-354 AND CYS-356.
[6]"The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases."
Snijder E.J., Wassenaar A.L.M., van Dinten L.C., Spaan W.J.M., Gorbalenya A.E.
J. Biol. Chem. 271:4864-4871(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, CHARACTERIZATION OF 3CLSP, MUTAGENESIS OF CYS-164; GLY-831; GLU-1064; HIS-1103; ASP-1117; ASP-1129; THR-1179; SER-1184; HIS-1198; GLU-1268; GLU-1430 AND GLU-1677.
[7]"An infectious arterivirus cDNA clone: identification of a replicase point mutation that abolishes discontinuous mRNA transcription."
van Dinten L.C., den Boon J.A., Wassenaar A.L.M., Spaan W.J.M., Snijder E.J.
Proc. Natl. Acad. Sci. U.S.A. 94:991-996(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-2429.
[8]"Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: evidence that NSP2 acts as a cofactor for the NSP4 serine protease."
Wassenaar A.L.M., Spaan W.J.M., Gorbalenya A.E., Snijder E.J.
J. Virol. 71:9313-9322(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, MUTAGENESIS OF GLU-1268.
[9]"ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex."
van der Meer Y., van Tol H., Locker J.K., Snijder E.J.
J. Virol. 72:6689-6698(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Proteolytic processing of the open reading frame 1b-encoded part of arterivirus replicase is mediated by nsp4 serine protease and is essential for virus replication."
van Dinten L.C., Rensen S., Gorbalenya A.E., Snijder E.J.
J. Virol. 73:2027-2037(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN 1B, MUTAGENESIS OF ASP-2351; GLU-2370; GLU-2800; ASP-2819; GLU-2835; GLN-2837 AND GLU-3056.
[11]"Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases."
Seybert A., van Dinten L.C., Snijder E.J., Ziebuhr J.
J. Virol. 74:9586-9593(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF HELICASE.
[12]"A zinc finger-containing papain-like protease couples subgenomic mRNA synthesis to genome translation in a positive-stranded RNA virus."
Tijms M.A., van Dinten L.C., Gorbalenya A.E., Snijder E.J.
Proc. Natl. Acad. Sci. U.S.A. 98:1889-1894(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: C4-TYPE ZINC-FINGER OF NSP1, MUTAGENESIS OF CYS-25 AND CYS-44.
[13]"Nuclear localization of non-structural protein 1 and nucleocapsid protein of equine arteritis virus."
Tijms M.A., van der Meer Y., Snijder E.J.
J. Gen. Virol. 83:795-800(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION OF NSP1 PAPAIN-LIKE CYSTEINE PROTEINASE.
[14]"Equine arteritis virus non-structural protein 1, an essential factor for viral subgenomic mRNA synthesis, interacts with the cellular transcription co-factor p100."
Tijms M.A., Snijder E.J.
J. Gen. Virol. 84:2317-2322(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN SND1/P100.
[15]"Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses."
Frias-Staheli N., Giannakopoulos N.V., Kikkert M., Taylor S.L., Bridgen A., Paragas J., Richt J.A., Rowland R.R., Schmaljohn C.S., Lenschow D.J., Snijder E.J., Garcia-Sastre A., Virgin H.W.
Cell Host Microbe 2:404-416(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF NSP2.
[16]"Identification of porcine reproductive and respiratory syndrome virus ORF1a-encoded non-structural proteins in virus-infected cells."
Li Y., Tas A., Snijder E.J., Fang Y.
J. Gen. Virol. 93:829-839(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN 1A, PROTEOLYTIC PROCESSING OF POLYPROTEIN 1B.
[17]"Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole."
Barrette-Ng I.H., Ng K.K.-S., Mark B.L., Van Aken D., Cherney M.M., Garen C., Kolodenko Y., Gorbalenya A.E., Snijder E.J., James M.N.G.
J. Biol. Chem. 277:39960-39966(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1071-1268 (NSP4).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53459 Genomic RNA. Translation: CAC42774.2.
X53459 Genomic RNA. Translation: CAC42775.2.
X52277 Genomic RNA. Translation: CAA36520.1.
PIRRRWVEV. A39925.
RefSeqNP_127506.1. NC_002532.2.
NP_127507.1. NC_002532.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MBMX-ray2.00A/B/C/D1071-1268[»]
2L8KNMR-A1454-1575[»]
4IUMX-ray1.45A261-392[»]
4N0NX-ray2.00A2371-2772[»]
4N0OX-ray2.65A/C/E/G2371-2772[»]
ProteinModelPortalP19811.
SMRP19811. Positions 1071-1268.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC33.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID921339.

Enzyme and pathway databases

BRENDA3.4.21.114. 6985.

Family and domain databases

Gene3D3.30.40.20. 1 hit.
InterProIPR027351. (+)RNA_virus_helicase_core_dom.
IPR008743. Arterivirus_Nsp2_C33.
IPR023338. Arterivirus_NSP4_peptidase.
IPR027355. AV_MBD_dom.
IPR008741. AV_PCPalpha.
IPR025773. AV_PCPbeta.
IPR023183. Chymotrypsin-like_domain3.
IPR022230. DUF3756.
IPR029323. EAV_nsp1.
IPR008760. EAV_peptidase_S32.
IPR027417. P-loop_NTPase.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF12581. DUF3756. 1 hit.
PF14754. IFR3_antag. 1 hit.
PF05412. Peptidase_C33. 1 hit.
PF05579. Peptidase_S32. 1 hit.
PF00680. RdRP_1. 1 hit.
PF01443. Viral_helicase1. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS51538. AV_CP. 1 hit.
PS51652. AV_MBD. 1 hit.
PS51493. AV_NSP4_PRO. 1 hit.
PS51539. AV_PCP_ALPHA. 1 hit.
PS51540. AV_PCP_BETA. 1 hit.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19811.

Entry information

Entry nameRPOA_EAVBU
AccessionPrimary (citable) accession number: P19811
Secondary accession number(s): Q88625, Q8QZQ5, Q91DM2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: April 13, 2004
Last modified: June 11, 2014
This is version 133 of the entry and version 3 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