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P19811

- RPOA_EAVBU

UniProt

P19811 - RPOA_EAVBU

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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Equine arteritis virus (strain Bucyrus) (EAV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication
Nsp1 is essential for viral subgenomic mRNA synthesis.1 Publication
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.1 Publication
The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.1 Publication
The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.1 Publication

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei164 – 1641For Nsp1 papain-like cysteine proteinase activity
Active sitei230 – 2301For Nsp1 papain-like cysteine proteinase activity
Sitei260 – 2612Cleavage; by PCP
Active sitei270 – 2701For Nsp2 cysteine proteinase activity
Active sitei332 – 3321For Nsp2 cysteine proteinase activity
Sitei831 – 8322Cleavage; by Nsp2 cysteine proteinase
Sitei1064 – 10652Cleavage; by 3CLSP
Active sitei1103 – 11031Charge relay system; for 3C-like serine proteinase activityPROSITE-ProRule annotation
Active sitei1129 – 11291Charge relay system; for 3C-like serine proteinase activityPROSITE-ProRule annotation
Active sitei1184 – 11841Charge relay system; for 3C-like serine proteinase activityPROSITE-ProRule annotation
Sitei1268 – 12692Cleavage; by 3CLSP; in major pathway
Sitei1430 – 14312Cleavage; by 3CLSP; in minor pathway
Sitei1452 – 14532Cleavage; by 3CLSP; in minor pathway
Sitei1575 – 15762Cleavage; by 3CLSP
Sitei1677 – 16782Cleavage; by 3CLSP
Sitei2370 – 23712Cleavage; by 3CLSP
Sitei2429 – 24291Involved in mRNA transcription process
Sitei2837 – 28382Cleavage; by 3CLSP
Sitei3056 – 30572Cleavage; by 3CLSP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri25 – 4420C4-type; atypicalAdd
BLAST
Nucleotide bindingi2528 – 25358ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. helicase activity Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. RNA binding Source: InterPro
  6. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  7. serine-type endopeptidase activity Source: InterPro
  8. serine-type exopeptidase activity Source: InterPro

GO - Biological processi

  1. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
  2. suppression by virus of host ISG15 activity Source: UniProtKB-KW
  3. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
  4. transcription, DNA-templated Source: InterPro
  5. viral protein processing Source: InterPro
  6. viral RNA genome replication Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase

Keywords - Biological processi

Host-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

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.21.114. 6985.

Protein family/group databases

MEROPSiC33.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Replicase polyprotein 1ab
Alternative name(s):
ORF1ab polyprotein
Cleaved into the following 14 chains:
Alternative name(s):
CP2
Short name:
CP
Non-structural protein 3
Short name:
Nsp3
3C-like serine proteinase (EC:3.4.21.-)
Short name:
3CLSP
Alternative name(s):
Nsp4
Non-structural protein 5-6-7
Short name:
Nsp5-6-7
Non-structural protein 5
Short name:
Nsp5
Non-structural protein 6
Short name:
Nsp6
Non-structural protein 7-alpha
Short name:
Nsp7-alpha
Non-structural protein 7-beta
Short name:
Nsp7-beta
Non-structural protein 8
Short name:
Nsp8
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
Pol
Short name:
RdRp
Alternative name(s):
Nsp9
Helicase (EC:3.6.4.12, EC:3.6.4.13)
Short name:
Hel
Alternative name(s):
Nsp10
Non-structural protein 11
Short name:
Nsp11
Non-structural protein 12
Short name:
Nsp12
Gene namesi
Name:rep
ORF Names:1a-1b
OrganismiEquine arteritis virus (strain Bucyrus) (EAV)
Taxonomic identifieri299386 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesArteriviridaeArterivirus
Virus hostiEquidae (horses) [TaxID: 9788]
ProteomesiUP000000353: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei530 – 55021HelicalSequence AnalysisAdd
BLAST
Transmembranei551 – 57121HelicalSequence AnalysisAdd
BLAST
Transmembranei625 – 64521HelicalSequence AnalysisAdd
BLAST
Transmembranei829 – 84921HelicalSequence AnalysisAdd
BLAST
Transmembranei903 – 92321HelicalSequence AnalysisAdd
BLAST
Transmembranei935 – 95521HelicalSequence AnalysisAdd
BLAST
Transmembranei977 – 99721HelicalSequence AnalysisAdd
BLAST
Transmembranei1291 – 131121HelicalSequence AnalysisAdd
BLAST
Transmembranei1333 – 135321HelicalSequence AnalysisAdd
BLAST
Transmembranei1355 – 137521HelicalSequence AnalysisAdd
BLAST
Transmembranei1385 – 140521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Host nucleus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251C → A: Complete loss of transcription. 1 Publication
Mutagenesisi44 – 441C → A: Complete loss of transcription. 1 Publication
Mutagenesisi164 – 1641C → G or S: Complete loss of PCP proteinase activity. 2 Publications
Mutagenesisi219 – 2191H → A, G or V: No effect. 1 Publication
Mutagenesisi230 – 2301H → A, G or V: Complete loss of PCP proteinase activity. 1 Publication
Mutagenesisi260 – 2601G → V: Complete loss of nsp1-nsp2 cleavage. 1 Publication
Mutagenesisi270 – 2701C → A, H, R or S: Complete loss of CP2 activity. 1 Publication
Mutagenesisi271 – 2711G → W: Complete loss of CP2 activity. 1 Publication
Mutagenesisi291 – 2911D → E or N: No effect. 1 Publication
Mutagenesisi295 – 2951D → E or N: No effect. 1 Publication
Mutagenesisi296 – 2961D → E or N: No effect. 1 Publication
Mutagenesisi297 – 2971E → D or Q: No effect. 1 Publication
Mutagenesisi319 – 3191C → A, H or P: Complete loss of CP2 activity. 1 Publication
Mutagenesisi332 – 3321H → C, I, N or Y: Complete loss of CP2 activity. 1 Publication
Mutagenesisi344 – 3441C → A: No effect. 1 Publication
Mutagenesisi344 – 3441C → H: Almost complete loss of CP2 activity. 1 Publication
Mutagenesisi349 – 3491C → A, H or S: Complete loss of CP2 activity. 1 Publication
Mutagenesisi354 – 3541C → A, H or P: Complete loss of CP2 activity. 1 Publication
Mutagenesisi356 – 3561C → A: Complete loss of CP2 activity. 1 Publication
Mutagenesisi356 – 3561C → H: No effect. 1 Publication
Mutagenesisi831 – 8311G → P: Complete loss of nsp2-nsp3 cleavage. 1 Publication
Mutagenesisi1064 – 10641E → P: Complete loss of nsp3-nsp4 cleavage. 1 Publication
Mutagenesisi1103 – 11031H → G or R: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication
Mutagenesisi1117 – 11171D → N or T: No effect. 1 Publication
Mutagenesisi1129 – 11291D → E: Complete loss of nsp3-nsp4 and nsp5-nsp6 cleavages. 1 Publication
Mutagenesisi1129 – 11291D → K or V: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication
Mutagenesisi1179 – 11791T → G or S: Partial loss of nsp4-nsp5 cleavage. 1 Publication
Mutagenesisi1179 – 11791T → N: Increased nsp5-nsp6 cleavage. 1 Publication
Mutagenesisi1184 – 11841S → C, F, I or T: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication
Mutagenesisi1198 – 11981H → L, R or Y: Complete loss of nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication
Mutagenesisi1268 – 12681E → P: Complete loss of nsp3-nsp4 and nsp4-nsp5 cleavages. 2 Publications
Mutagenesisi1430 – 14301E → P: No effect. 1 Publication
Mutagenesisi1677 – 16771E → P: Complete loss of nsp5-nsp6 cleavage. 1 Publication
Mutagenesisi2351 – 23511D → P: No effect. 1 Publication
Mutagenesisi2370 – 23701E → P: Complete loss of nsp9-nsp10 cleavage. 1 Publication
Mutagenesisi2429 – 24291S → P: RNA can replicate efficiently but does not produce the subgenomic mRNAs required for structural protein expression. 1 Publication
Mutagenesisi2800 – 28001E → P: No effect. 1 Publication
Mutagenesisi2819 – 28191D → P: No effect. 1 Publication
Mutagenesisi2835 – 28351E → D, P or Q: Almost complete loss of nsp9-nsp10 cleavage. 1 Publication
Mutagenesisi2837 – 28371Q → D or N: No effect. 1 Publication
Mutagenesisi2837 – 28371Q → E: Increased nsp9-nsp10 cleavage. 1 Publication
Mutagenesisi2837 – 28371Q → P: Almost complete loss of nsp9-nsp10 cleavage. 1 Publication
Mutagenesisi3056 – 30561E → P: Complete loss of nsp10-nsp11 cleavage. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31753175Replicase polyprotein 1abPRO_0000036619Add
BLAST
Chaini1 – 260260Nsp1 papain-like cysteine proteinasePRO_0000036621Add
BLAST
Chaini261 – 831571Nsp2 cysteine proteinasePRO_0000036622Add
BLAST
Chaini832 – 1064233Non-structural protein 3PRO_0000036623Add
BLAST
Chaini1065 – 12682043C-like serine proteinasePRO_0000036624Add
BLAST
Chaini1269 – 1677409Non-structural protein 5-6-7PRO_0000036625Add
BLAST
Chaini1269 – 1430162Non-structural protein 5PRO_0000423106Add
BLAST
Chaini1431 – 145222Non-structural protein 6PRO_0000423107Add
BLAST
Chaini1453 – 1575123Non-structural protein 7-alphaPRO_0000423108Add
BLAST
Chaini1576 – 1677102Non-structural protein 7-betaPRO_0000423109Add
BLAST
Chaini1678 – 2370693RNA-directed RNA polymerasePRO_0000036626Add
BLAST
Chaini1678 – 172750Non-structural protein 8PRO_0000036627Add
BLAST
Chaini2371 – 2837467HelicasePRO_0000036628Add
BLAST
Chaini2838 – 3056219Non-structural protein 11PRO_0000036629Add
BLAST
Chaini3057 – 3175119Non-structural protein 12PRO_0000036630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi1501 – 15011N-linked (GlcNAc...); by hostCurated

Post-translational modificationi

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 nsp4.5 Publications

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Nsp1 interacts with cellular transcription cofactor SND1/p100.1 Publication

Structurei

Secondary structure

1
3175
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi270 – 2778Combined sources
Turni278 – 2803Combined sources
Beta strandi283 – 2864Combined sources
Helixi290 – 2923Combined sources
Helixi296 – 30510Combined sources
Beta strandi309 – 3124Combined sources
Beta strandi323 – 3297Combined sources
Beta strandi332 – 3376Combined sources
Helixi347 – 3515Combined sources
Helixi369 – 37911Combined sources
Turni380 – 3823Combined sources
Beta strandi383 – 3864Combined sources
Beta strandi1076 – 109217Combined sources
Beta strandi1095 – 11017Combined sources
Helixi1102 – 11054Combined sources
Beta strandi1110 – 11156Combined sources
Beta strandi1118 – 11236Combined sources
Beta strandi1125 – 11273Combined sources
Beta strandi1130 – 11356Combined sources
Turni1137 – 11393Combined sources
Beta strandi1154 – 11618Combined sources
Beta strandi1164 – 11707Combined sources
Helixi1181 – 11833Combined sources
Beta strandi1187 – 11904Combined sources
Beta strandi1193 – 120210Combined sources
Helixi1203 – 12053Combined sources
Beta strandi1206 – 12105Combined sources
Beta strandi1216 – 12205Combined sources
Helixi1224 – 12285Combined sources
Beta strandi1233 – 12375Combined sources
Beta strandi1250 – 12545Combined sources
Helixi1255 – 12628Combined sources
Turni1454 – 14596Combined sources
Helixi1463 – 147412Combined sources
Beta strandi1476 – 14805Combined sources
Beta strandi1483 – 14864Combined sources
Helixi1490 – 150617Combined sources
Helixi1510 – 152011Combined sources
Turni1521 – 15244Combined sources
Beta strandi1533 – 15397Combined sources
Beta strandi1545 – 15484Combined sources
Beta strandi1551 – 156010Combined sources
Beta strandi1565 – 15739Combined sources
Turni2375 – 23773Combined sources
Beta strandi2382 – 23854Combined sources
Turni2393 – 23953Combined sources
Helixi2396 – 23994Combined sources
Beta strandi2400 – 24034Combined sources
Beta strandi2405 – 24095Combined sources
Helixi2416 – 24183Combined sources
Beta strandi2419 – 24235Combined sources
Turni2424 – 24285Combined sources
Helixi2440 – 245112Combined sources
Beta strandi2457 – 24626Combined sources
Beta strandi2465 – 24684Combined sources
Beta strandi2470 – 24756Combined sources
Beta strandi2478 – 24836Combined sources
Beta strandi2488 – 24947Combined sources
Beta strandi2496 – 25038Combined sources
Helixi2513 – 25219Combined sources
Beta strandi2524 – 25274Combined sources
Helixi2534 – 254411Combined sources
Beta strandi2549 – 25524Combined sources
Helixi2556 – 256813Combined sources
Beta strandi2591 – 25966Combined sources
Beta strandi2605 – 26095Combined sources
Turni2610 – 26145Combined sources
Helixi2617 – 262610Combined sources
Beta strandi2630 – 26334Combined sources
Turni2648 – 26514Combined sources
Helixi2652 – 26543Combined sources
Beta strandi2655 – 26573Combined sources
Beta strandi2665 – 26673Combined sources
Helixi2669 – 26746Combined sources
Turni2675 – 26784Combined sources
Beta strandi2690 – 26934Combined sources
Beta strandi2702 – 27087Combined sources
Helixi2709 – 27113Combined sources
Beta strandi2717 – 27193Combined sources
Helixi2720 – 27223Combined sources
Beta strandi2727 – 27337Combined sources
Beta strandi2736 – 27383Combined sources
Helixi2742 – 27487Combined sources
Beta strandi2750 – 275910Combined sources
Helixi2765 – 27684Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP19811.
SMRiP19811. Positions 1071-1268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19811.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 15691Peptidase C31PROSITE-ProRule annotationAdd
BLAST
Domaini157 – 260104Peptidase C32PROSITE-ProRule annotationAdd
BLAST
Domaini261 – 360100Peptidase C33PROSITE-ProRule annotationAdd
BLAST
Domaini1065 – 1268204Peptidase S32PROSITE-ProRule annotationAdd
BLAST
Domaini2116 – 2251136RdRp catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini2371 – 243868AV MBDAdd
BLAST
Domaini2496 – 2661166(+)RNA virus helicase ATP-bindingAdd
BLAST
Domaini2662 – 2793132(+)RNA virus helicase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni261 – 33979OTU-likeAdd
BLAST
Regioni530 – 645116HD1Add
BLAST
Regioni829 – 997169HD2Add
BLAST
Regioni1291 – 1405115HD3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi389 – 44052Pro-richAdd
BLAST

Domaini

The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.
The OTU-like region is responsible for the deubiquitinating and deISGylation activities of Nsp2.Curated

Sequence similaritiesi

Belongs to the arteriviridae polyprotein family.Curated
Contains 1 peptidase C31 domain.PROSITE-ProRule annotation
Contains 1 peptidase C32 domain.PROSITE-ProRule annotation
Contains 1 peptidase C33 domain.PROSITE-ProRule annotation
Contains 1 peptidase S32 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri25 – 4420C4-type; atypicalAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.30.40.20. 1 hit.
InterProiIPR027351. (+)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]
PfamiPF12581. 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]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51538. 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]

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 1ab (identifier: P19811-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATFSATGFG GSFVRDWSLD LPDACEHGAG LCCEVDGSTL CAECFRGCEG
60 70 80 90 100
MEQCPGLFMG LLKLASPVPV GHKFLIGWYR AAKVTGRYNF LELLQHPAFA
110 120 130 140 150
QLRVVDARLA IEEASVFIST DHASAKRFPG ARFALTPVYA NAWVVSPAAN
160 170 180 190 200
SLIVTTDQEQ DGFCWLKLLP PDRREAGLRL YYNHYREQRT GWLSKTGLRL
210 220 230 240 250
WLGDLGLGIN ASSGGLKFHI MRGSPQRAWH ITTRSCKLKS YYVCDISEAD
260 270 280 290 300
WSCLPAGNYG GYNPPGDGAC GYRCLAFMNG ATVVSAGCSS DLWCDDELAY
310 320 330 340 350
RVFQLSPTFT VTIPGGRVCP NAKYAMICDK QHWRVKRAKG VGLCLDESCF
360 370 380 390 400
RGICNCQRMS GPPPAPVSAA VLDHILEAAT FGNVRVVTPE GQPRPVPAPR
410 420 430 440 450
VRPSANSSGD VKDPAPVPPV PKPRTKLATP NPTQAPIPAP RTRLQGASTQ
460 470 480 490 500
EPLASAGVAS DSAPKWRVAK TVYSSAERFR TELVQRARSV GDVLVQALPL
510 520 530 540 550
KTPAVQRYTM TLKMMRSRFS WHCDVWYPLA VIACLLPIWP SLALLLSFAI
560 570 580 590 600
GLIPSVGNNV VLTALLVSSA NYVASMDHQC EGAACLALLE EEHYYRAVRW
610 620 630 640 650
RPITGALSLV LNLLGQVGYV ARSTFDAAYV PCTVFDLCSF AILYLCRNRC
660 670 680 690 700
WRCFGRCVRV GPATHVLGST GQRVSKLALI DLCDHFSKPT IDVVGMATGW
710 720 730 740 750
SGCYTGTAAM ERQCASTVDP HSFDQKKAGA TVYLTPPVNS GSALQCLNVM
760 770 780 790 800
WKRPIGSTVL GEQTGAVVTA VKSISFSPPC CVSTTLPTRP GVTVVDHALY
810 820 830 840 850
NRLTASGVDP ALLRVGQGDF LKLNPGFRLI GGWIYGICYF VLVVVSTFTC
860 870 880 890 900
LPIKCGIGTR DPFCRRVFSV PVTKTQEHCH AGMCASAEGI SLDSLGLTQL
910 920 930 940 950
QSYWIAAVTS GLVILLVCHR LAISALDLLT LASPLVLLVF PWASVGLLLA
960 970 980 990 1000
CSLAGAAVKI QLLATLFVNL FFPQATLVTM GYWACVAALA VYSLMGLRVK
1010 1020 1030 1040 1050
VNVPMCVTPA HFLLLARSAG QSREQMLRVS AAAPTNSLLG VARDCYVTGT
1060 1070 1080 1090 1100
TRLYIPKEGG MVFEGLFRSP KARGNVGFVA GSSYGTGSVW TRNNEVVVLT
1110 1120 1130 1140 1150
ASHVVGRANM ATLKIGDAML TLTFKKNGDF AEAVTTQSEL PGNWPQLHFA
1160 1170 1180 1190 1200
QPTTGPASWC TATGDEEGLL SGEVCLAWTT SGDSGSAVVQ GDAVVGVHTG
1210 1220 1230 1240 1250
SNTSGVAYVT TPSGKLLGAD TVTLSSLSKH FTGPLTSIPK DIPDNIIADV
1260 1270 1280 1290 1300
DAVPRSLAML IDGLSNRESS LSGPQLLLIA CFMWSYLNQP AYLPYVLGFF
1310 1320 1330 1340 1350
AANFFLPKSV GRPVVTGLLW LCCLFTPLSM RLCLFHLVCA TVTGNVISLW
1360 1370 1380 1390 1400
FYITAAGTSY LSEMWFGGYP TMLFVPRFLV YQFPGWAIGT VLAVCSITML
1410 1420 1430 1440 1450
AAALGHTLLL DVFSASGRFD RTFMMKYFLE GGVKESVTAS VTRAYGKPIT
1460 1470 1480 1490 1500
QESLTATLAA LTDDDFQFLS DVLDCRAVRS AMNLRAALTS FQVAQYRNIL
1510 1520 1530 1540 1550
NASLQVDRDA ARSRRLMAKL ADFAVEQEVT AGDRVVVIDG LDRMAHFKDD
1560 1570 1580 1590 1600
LVLVPLTTKV VGGSRCTICD VVKEEANDTP VKPMPSRRRR KGLPKGAQLE
1610 1620 1630 1640 1650
WDRHQEEKRN AGDDDFAVSN DYVKRVPKYW DPSDTRGTTV KIAGTTYQKV
1660 1670 1680 1690 1700
VDYSGNVHYV EHQEDLLDYV LGKGSYEGLD QDKVLDLTNM LKVDPTELSS
1710 1720 1730 1740 1750
KDKAKARQLA HLLLDLANPV EAVNQLNLRA PHIFPGDVGR RTFADSKDKG
1760 1770 1780 1790 1800
FVALHSRTMF LAARDFLFNI KFVCDEEFTK TPKDTLLGYV RACPGYWFIF
1810 1820 1830 1840 1850
RRTHRSLIDA YWDSMECVYA LPTISDFDVS PGDVAVTGER WDFESPGGGR
1860 1870 1880 1890 1900
AKRLTADLVH AFQGFHGASY SYDDKVAAAV SGDPYRSDGV LYNTRWGNIP
1910 1920 1930 1940 1950
YSVPTNALEA TACYRAGCEA VTDGTNVIAT IGPFPEQQPI PDIPKSVLDN
1960 1970 1980 1990 2000
CADISCDAFI APAAETALCG DLEKYNLSTQ GFVLPSVFSM VRAYLKEEIG
2010 2020 2030 2040 2050
DAPPLYLPST VPSKNSQAGI NGAEFPTKSL QSYCLIDDMV SQSMKSNLQT
2060 2070 2080 2090 2100
ATMATCKRQY CSKYKIRSIL GTNNYIGLGL RACLSGVTAA FQKAGKDGSP
2110 2120 2130 2140 2150
IYLGKSKFDP IPAPDKYCLE TDLESCDRST PALVRWFATN LIFELAGQPE
2160 2170 2180 2190 2200
LVHSYVLNCC HDLVVAGSVA FTKRGGLSSG DPITSISNTI YSLVLYTQHM
2210 2220 2230 2240 2250
LLCGLEGYFP EIAEKYLDGS LELRDMFKYV RVYIYSDDVV LTTPNQHYAA
2260 2270 2280 2290 2300
SFDRWVPHLQ ALLGFKVDPK KTVNTSSPSF LGCRFKQVDG KCYLASLQDR
2310 2320 2330 2340 2350
VTRSLLYHIG AKNPSEYYEA AVSIFKDSII CCDEDWWTDL HRRISGAART
2360 2370 2380 2390 2400
DGVEFPTIEM LTSFRTKQYE SAVCTVCGAA PVAKSACGGW FCGNCVPYHA
2410 2420 2430 2440 2450
GHCHTTSLFA NCGHDIMYRS TYCTMCEGSP KQMVPKVPHP ILDHLLCHID
2460 2470 2480 2490 2500
YGSKEELTLV VADGRTTSPP GRYKVGHKVV AVVADVGGNI VFGCGPGSHI
2510 2520 2530 2540 2550
AVPLQDTLKG VVVNKALKNA AASEYVEGPP GSGKTFHLVK DVLAVVGSAT
2560 2570 2580 2590 2600
LVVPTHASML DCINKLKQAG ADPYFVVPKY TVLDFPRPGS GNITVRLPQV
2610 2620 2630 2640 2650
GTSEGETFVD EVAYFSPVDL ARILTQGRVK GYGDLNQLGC VGPASVPRNL
2660 2670 2680 2690 2700
WLRHFVSLEP LRVCHRFGAA VCDLIKGIYP YYEPAPHTTK VVFVPNPDFE
2710 2720 2730 2740 2750
KGVVITAYHK DRGLGHRTID SIQGCTFPVV TLRLPTPQSL TRPRAVVAVT
2760 2770 2780 2790 2800
RASQELYIYD PFDQLSGLLK FTKEAEAQDL IHGPPTACHL GQEIDLWSNE
2810 2820 2830 2840 2850
GLEYYKEVNL LYTHVPIKDG VIHSYPNCGP ACGWEKQSNK ISCLPRVAQN
2860 2870 2880 2890 2900
LGYHYSPDLP GFCPIPKELA EHWPVVSNDR YPNCLQITLQ QVCELSKPCS
2910 2920 2930 2940 2950
AGYMVGQSVF VQTPGVTSYW LTEWVDGKAR ALPDSLFSSG RFETNSRAFL
2960 2970 2980 2990 3000
DEAEEKFAAA HPHACLGEIN KSTVGGSHFI FSQYLPPLLP ADAVALVGAS
3010 3020 3030 3040 3050
LAGKAAKAAC SVVDVYAPSF EPYLHPETLS RVYKIMIDFK PCRLMVWRNA
3060 3070 3080 3090 3100
TFYVQEGVDA VTSALAAVSK LIKVPANEPV SFHVASGYRT NALVAPQAKI
3110 3120 3130 3140 3150
SIGAYAAEWA LSTEPPPAGY AIVRRYIVKR LLSSTEVFLC RRGVVSSTSV
3160 3170
QTICALEGCK PLFNFLQIGS VIGPV

Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.

Length:3,175
Mass (Da):345,384
Last modified:April 13, 2004 - v3
Checksum:iCB536C1F5091045C
GO
Isoform Replicase polyprotein 1a (identifier: P19811-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,727
Mass (Da):186,992
Checksum:iFB0DB046FA0C74F6
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1728 – 31751448Missing in isoform Replicase polyprotein 1a. CuratedVSP_032887Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53459 Genomic RNA. Translation: CAC42774.2.
X53459 Genomic RNA. Translation: CAC42775.2.
X52277 Genomic RNA. Translation: CAA36520.1.
PIRiA39925. RRWVEV.
RefSeqiNP_127506.1. NC_002532.2.
NP_127507.1. NC_002532.2.

Genome annotation databases

GeneIDi921339.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53459 Genomic RNA. Translation: CAC42774.2 .
X53459 Genomic RNA. Translation: CAC42775.2 .
X52277 Genomic RNA. Translation: CAA36520.1 .
PIRi A39925. RRWVEV.
RefSeqi NP_127506.1. NC_002532.2.
NP_127507.1. NC_002532.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MBM X-ray 2.00 A/B/C/D 1071-1268 [» ]
2L8K NMR - A 1454-1575 [» ]
4IUM X-ray 1.45 A 261-392 [» ]
4N0N X-ray 2.00 A 2371-2772 [» ]
4N0O X-ray 2.65 A/C/E/G 2371-2772 [» ]
ProteinModelPortali P19811.
SMRi P19811. Positions 1071-1268.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C33.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 921339.

Enzyme and pathway databases

BRENDAi 3.4.21.114. 6985.

Miscellaneous databases

EvolutionaryTracei P19811.

Family and domain databases

Gene3Di 3.30.40.20. 1 hit.
InterProi IPR027351. (+)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 ]
Pfami PF12581. 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 ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS51538. 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 ]
ProtoNeti Search...

Publicationsi

  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. 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).

Entry informationi

Entry nameiRPOA_EAVBU
AccessioniPrimary (citable) accession number: P19811
Secondary accession number(s): Q88625, Q8QZQ5, Q91DM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: April 13, 2004
Last modified: November 26, 2014
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, 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