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P19811

- RPOA_EAVBU

UniProt

P19811 - RPOA_EAVBU

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
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 3 (13 Apr 2004)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

    1. host cell membrane Source: UniProtKB-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell
    3. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Transmembrane

    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

    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

    MATFSATGFG GSFVRDWSLD LPDACEHGAG LCCEVDGSTL CAECFRGCEG     50
    MEQCPGLFMG LLKLASPVPV GHKFLIGWYR AAKVTGRYNF LELLQHPAFA 100
    QLRVVDARLA IEEASVFIST DHASAKRFPG ARFALTPVYA NAWVVSPAAN 150
    SLIVTTDQEQ DGFCWLKLLP PDRREAGLRL YYNHYREQRT GWLSKTGLRL 200
    WLGDLGLGIN ASSGGLKFHI MRGSPQRAWH ITTRSCKLKS YYVCDISEAD 250
    WSCLPAGNYG GYNPPGDGAC GYRCLAFMNG ATVVSAGCSS DLWCDDELAY 300
    RVFQLSPTFT VTIPGGRVCP NAKYAMICDK QHWRVKRAKG VGLCLDESCF 350
    RGICNCQRMS GPPPAPVSAA VLDHILEAAT FGNVRVVTPE GQPRPVPAPR 400
    VRPSANSSGD VKDPAPVPPV PKPRTKLATP NPTQAPIPAP RTRLQGASTQ 450
    EPLASAGVAS DSAPKWRVAK TVYSSAERFR TELVQRARSV GDVLVQALPL 500
    KTPAVQRYTM TLKMMRSRFS WHCDVWYPLA VIACLLPIWP SLALLLSFAI 550
    GLIPSVGNNV VLTALLVSSA NYVASMDHQC EGAACLALLE EEHYYRAVRW 600
    RPITGALSLV LNLLGQVGYV ARSTFDAAYV PCTVFDLCSF AILYLCRNRC 650
    WRCFGRCVRV GPATHVLGST GQRVSKLALI DLCDHFSKPT IDVVGMATGW 700
    SGCYTGTAAM ERQCASTVDP HSFDQKKAGA TVYLTPPVNS GSALQCLNVM 750
    WKRPIGSTVL GEQTGAVVTA VKSISFSPPC CVSTTLPTRP GVTVVDHALY 800
    NRLTASGVDP ALLRVGQGDF LKLNPGFRLI GGWIYGICYF VLVVVSTFTC 850
    LPIKCGIGTR DPFCRRVFSV PVTKTQEHCH AGMCASAEGI SLDSLGLTQL 900
    QSYWIAAVTS GLVILLVCHR LAISALDLLT LASPLVLLVF PWASVGLLLA 950
    CSLAGAAVKI QLLATLFVNL FFPQATLVTM GYWACVAALA VYSLMGLRVK 1000
    VNVPMCVTPA HFLLLARSAG QSREQMLRVS AAAPTNSLLG VARDCYVTGT 1050
    TRLYIPKEGG MVFEGLFRSP KARGNVGFVA GSSYGTGSVW TRNNEVVVLT 1100
    ASHVVGRANM ATLKIGDAML TLTFKKNGDF AEAVTTQSEL PGNWPQLHFA 1150
    QPTTGPASWC TATGDEEGLL SGEVCLAWTT SGDSGSAVVQ GDAVVGVHTG 1200
    SNTSGVAYVT TPSGKLLGAD TVTLSSLSKH FTGPLTSIPK DIPDNIIADV 1250
    DAVPRSLAML IDGLSNRESS LSGPQLLLIA CFMWSYLNQP AYLPYVLGFF 1300
    AANFFLPKSV GRPVVTGLLW LCCLFTPLSM RLCLFHLVCA TVTGNVISLW 1350
    FYITAAGTSY LSEMWFGGYP TMLFVPRFLV YQFPGWAIGT VLAVCSITML 1400
    AAALGHTLLL DVFSASGRFD RTFMMKYFLE GGVKESVTAS VTRAYGKPIT 1450
    QESLTATLAA LTDDDFQFLS DVLDCRAVRS AMNLRAALTS FQVAQYRNIL 1500
    NASLQVDRDA ARSRRLMAKL ADFAVEQEVT AGDRVVVIDG LDRMAHFKDD 1550
    LVLVPLTTKV VGGSRCTICD VVKEEANDTP VKPMPSRRRR KGLPKGAQLE 1600
    WDRHQEEKRN AGDDDFAVSN DYVKRVPKYW DPSDTRGTTV KIAGTTYQKV 1650
    VDYSGNVHYV EHQEDLLDYV LGKGSYEGLD QDKVLDLTNM LKVDPTELSS 1700
    KDKAKARQLA HLLLDLANPV EAVNQLNLRA PHIFPGDVGR RTFADSKDKG 1750
    FVALHSRTMF LAARDFLFNI KFVCDEEFTK TPKDTLLGYV RACPGYWFIF 1800
    RRTHRSLIDA YWDSMECVYA LPTISDFDVS PGDVAVTGER WDFESPGGGR 1850
    AKRLTADLVH AFQGFHGASY SYDDKVAAAV SGDPYRSDGV LYNTRWGNIP 1900
    YSVPTNALEA TACYRAGCEA VTDGTNVIAT IGPFPEQQPI PDIPKSVLDN 1950
    CADISCDAFI APAAETALCG DLEKYNLSTQ GFVLPSVFSM VRAYLKEEIG 2000
    DAPPLYLPST VPSKNSQAGI NGAEFPTKSL QSYCLIDDMV SQSMKSNLQT 2050
    ATMATCKRQY CSKYKIRSIL GTNNYIGLGL RACLSGVTAA FQKAGKDGSP 2100
    IYLGKSKFDP IPAPDKYCLE TDLESCDRST PALVRWFATN LIFELAGQPE 2150
    LVHSYVLNCC HDLVVAGSVA FTKRGGLSSG DPITSISNTI YSLVLYTQHM 2200
    LLCGLEGYFP EIAEKYLDGS LELRDMFKYV RVYIYSDDVV LTTPNQHYAA 2250
    SFDRWVPHLQ ALLGFKVDPK KTVNTSSPSF LGCRFKQVDG KCYLASLQDR 2300
    VTRSLLYHIG AKNPSEYYEA AVSIFKDSII CCDEDWWTDL HRRISGAART 2350
    DGVEFPTIEM LTSFRTKQYE SAVCTVCGAA PVAKSACGGW FCGNCVPYHA 2400
    GHCHTTSLFA NCGHDIMYRS TYCTMCEGSP KQMVPKVPHP ILDHLLCHID 2450
    YGSKEELTLV VADGRTTSPP GRYKVGHKVV AVVADVGGNI VFGCGPGSHI 2500
    AVPLQDTLKG VVVNKALKNA AASEYVEGPP GSGKTFHLVK DVLAVVGSAT 2550
    LVVPTHASML DCINKLKQAG ADPYFVVPKY TVLDFPRPGS GNITVRLPQV 2600
    GTSEGETFVD EVAYFSPVDL ARILTQGRVK GYGDLNQLGC VGPASVPRNL 2650
    WLRHFVSLEP LRVCHRFGAA VCDLIKGIYP YYEPAPHTTK VVFVPNPDFE 2700
    KGVVITAYHK DRGLGHRTID SIQGCTFPVV TLRLPTPQSL TRPRAVVAVT 2750
    RASQELYIYD PFDQLSGLLK FTKEAEAQDL IHGPPTACHL GQEIDLWSNE 2800
    GLEYYKEVNL LYTHVPIKDG VIHSYPNCGP ACGWEKQSNK ISCLPRVAQN 2850
    LGYHYSPDLP GFCPIPKELA EHWPVVSNDR YPNCLQITLQ QVCELSKPCS 2900
    AGYMVGQSVF VQTPGVTSYW LTEWVDGKAR ALPDSLFSSG RFETNSRAFL 2950
    DEAEEKFAAA HPHACLGEIN KSTVGGSHFI FSQYLPPLLP ADAVALVGAS 3000
    LAGKAAKAAC SVVDVYAPSF EPYLHPETLS RVYKIMIDFK PCRLMVWRNA 3050
    TFYVQEGVDA VTSALAAVSK LIKVPANEPV SFHVASGYRT NALVAPQAKI 3100
    SIGAYAAEWA LSTEPPPAGY AIVRRYIVKR LLSSTEVFLC RRGVVSSTSV 3150
    QTICALEGCK PLFNFLQIGS VIGPV 3175

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 134 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