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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Equine arteritis virus (strain Bucyrus) (EAV)
Status
Reviewed-Annotation score: 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.2 Publications

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
ATP + H2O = ADP + phosphate.1 Publication
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)DescriptionActionsGraphical viewLength
Active sitei164For Nsp1 papain-like cysteine proteinase activity2 Publications1
Active sitei230For Nsp1 papain-like cysteine proteinase activity1 Publication1
Active sitei270For Nsp2 cysteine proteinase activity1 Publication1
Metal bindingi319Zinc 1Combined sources1
Active sitei332For Nsp2 cysteine proteinase activity1 Publication1
Metal bindingi349Zinc 1Combined sources1
Metal bindingi354Zinc 1Combined sources1
Metal bindingi356Zinc 1Combined sources1
Active sitei1103Charge relay system; for 3C-like serine proteinase activityPROSITE-ProRule annotation1
Active sitei1129Charge relay system; for 3C-like serine proteinase activityPROSITE-ProRule annotation1
Active sitei1184Charge relay system; for 3C-like serine proteinase activityPROSITE-ProRule annotation1
Metal bindingi2374Zinc 2PROSITE-ProRule annotationCombined sources1
Metal bindingi2377Zinc 2PROSITE-ProRule annotationCombined sources1
Metal bindingi2387Zinc 3PROSITE-ProRule annotationCombined sources1
Metal bindingi2392Zinc 2PROSITE-ProRule annotationCombined sources1
Metal bindingi2395Zinc 2PROSITE-ProRule annotationCombined sources1
Metal bindingi2399Zinc 3; via tele nitrogenPROSITE-ProRule annotationCombined sources1
Metal bindingi2402Zinc 3; via pros nitrogenPROSITE-ProRule annotationCombined sources1
Metal bindingi2403Zinc 3PROSITE-ProRule annotationCombined sources1
Metal bindingi2412Zinc 4PROSITE-ProRule annotationCombined sources1
Metal bindingi2414Zinc 4; via pros nitrogenPROSITE-ProRule annotationCombined sources1
Metal bindingi2423Zinc 4PROSITE-ProRule annotationCombined sources1
Metal bindingi2426Zinc 4PROSITE-ProRule annotationCombined sources1
Sitei2429Involved in mRNA transcription process1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri25 – 44C4-type; atypicalAdd BLAST20
Nucleotide bindingi2528 – 2535ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

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:
Nsp1 papain-like cysteine proteinase (EC:3.4.22.-2 Publications)
Short name:
PCP
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
Helicase2 Publications (EC:3.6.4.121 Publication, EC:3.6.4.131 Publication)
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 virusesssRNA positive-strand viruses, no DNA stageNidoviralesArteriviridaeArterivirus
Virus hostiEquidae (horses) [TaxID: 9788]
Proteomesi
  • UP000000353 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei530 – 550HelicalSequence analysisAdd BLAST21
Transmembranei551 – 571HelicalSequence analysisAdd BLAST21
Transmembranei625 – 645HelicalSequence analysisAdd BLAST21
Transmembranei829 – 849HelicalSequence analysisAdd BLAST21
Transmembranei903 – 923HelicalSequence analysisAdd BLAST21
Transmembranei935 – 955HelicalSequence analysisAdd BLAST21
Transmembranei977 – 997HelicalSequence analysisAdd BLAST21
Transmembranei1291 – 1311HelicalSequence analysisAdd BLAST21
Transmembranei1333 – 1353HelicalSequence analysisAdd BLAST21
Transmembranei1355 – 1375HelicalSequence analysisAdd BLAST21
Transmembranei1385 – 1405HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Host nucleus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi25C → A: Complete loss of transcription. 1 Publication1
Mutagenesisi44C → A: Complete loss of transcription. 1 Publication1
Mutagenesisi164C → G or S: Complete loss of PCP proteinase activity. 2 Publications1
Mutagenesisi219H → A, G or V: No effect. 1 Publication1
Mutagenesisi230H → A, G or V: Complete loss of PCP proteinase activity. 1 Publication1
Mutagenesisi260G → V: Complete loss of nsp1-nsp2 cleavage. 1 Publication1
Mutagenesisi270C → A, H, R or S: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi271G → W: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi291D → E or N: No effect. 1 Publication1
Mutagenesisi295D → E or N: No effect. 1 Publication1
Mutagenesisi296D → E or N: No effect. 1 Publication1
Mutagenesisi297E → D or Q: No effect. 1 Publication1
Mutagenesisi319C → A, H or P: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi332H → C, I, N or Y: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi344C → A: No effect. 1 Publication1
Mutagenesisi344C → H: Almost complete loss of CP2 activity. 1 Publication1
Mutagenesisi349C → A, H or S: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi354C → A, H or P: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi356C → A: Complete loss of CP2 activity. 1 Publication1
Mutagenesisi356C → H: No effect. 1 Publication1
Mutagenesisi831G → P: Complete loss of nsp2-nsp3 cleavage. 1 Publication1
Mutagenesisi1064E → P: Complete loss of nsp3-nsp4 cleavage. 1 Publication1
Mutagenesisi1103H → G or R: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1117D → N or T: No effect. 1 Publication1
Mutagenesisi1129D → E: Complete loss of nsp3-nsp4 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1129D → K or V: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1179T → G or S: Partial loss of nsp4-nsp5 cleavage. 1 Publication1
Mutagenesisi1179T → N: Increased nsp5-nsp6 cleavage. 1 Publication1
Mutagenesisi1184S → C, F, I or T: Complete loss of nsp3-nsp4, nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1198H → L, R or Y: Complete loss of nsp4-nsp5 and nsp5-nsp6 cleavages. 1 Publication1
Mutagenesisi1268E → P: Complete loss of nsp3-nsp4 and nsp4-nsp5 cleavages. 2 Publications1
Mutagenesisi1430E → P: No effect. 1 Publication1
Mutagenesisi1677E → P: Complete loss of nsp5-nsp6 cleavage. 1 Publication1
Mutagenesisi2351D → P: No effect. 1 Publication1
Mutagenesisi2370E → P: Complete loss of nsp9-nsp10 cleavage. 1 Publication1
Mutagenesisi2429S → P: RNA can replicate efficiently but does not produce the subgenomic mRNAs required for structural protein expression. 1 Publication1
Mutagenesisi2534K → Q: Abolishes ATPase and helicase activity. 1 Publication1
Mutagenesisi2800E → P: No effect. 1 Publication1
Mutagenesisi2819D → P: No effect. 1 Publication1
Mutagenesisi2835E → D, P or Q: Almost complete loss of nsp9-nsp10 cleavage. 1 Publication1
Mutagenesisi2837Q → D or N: No effect. 1 Publication1
Mutagenesisi2837Q → E: Increased nsp9-nsp10 cleavage. 1 Publication1
Mutagenesisi2837Q → P: Almost complete loss of nsp9-nsp10 cleavage. 1 Publication1
Mutagenesisi3056E → P: Complete loss of nsp10-nsp11 cleavage. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000366191 – 3175Replicase polyprotein 1abAdd BLAST3175
ChainiPRO_00000366211 – 260Nsp1 papain-like cysteine proteinaseAdd BLAST260
ChainiPRO_0000036622261 – 831Nsp2 cysteine proteinaseAdd BLAST571
ChainiPRO_0000036623832 – 1064Non-structural protein 3Add BLAST233
ChainiPRO_00000366241065 – 12683C-like serine proteinaseAdd BLAST204
ChainiPRO_00000366251269 – 1677Non-structural protein 5-6-7Add BLAST409
ChainiPRO_00004231061269 – 1430Non-structural protein 5Add BLAST162
ChainiPRO_00004231071431 – 1452Non-structural protein 6Add BLAST22
ChainiPRO_00004231081453 – 1575Non-structural protein 7-alphaAdd BLAST123
ChainiPRO_00004231091576 – 1677Non-structural protein 7-betaAdd BLAST102
ChainiPRO_00000366261678 – 2370RNA-directed RNA polymeraseAdd BLAST693
ChainiPRO_00000366271678 – 1727Non-structural protein 8Add BLAST50
ChainiPRO_00000366282371 – 2837HelicaseAdd BLAST467
ChainiPRO_00000366292838 – 3056Non-structural protein 11Add BLAST219
ChainiPRO_00000366303057 – 3175Non-structural protein 12Add BLAST119

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi1501N-linked (GlcNAc...); by hostCurated1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei260 – 261Cleavage; by PCP2
Sitei831 – 832Cleavage; by Nsp2 cysteine proteinase2
Sitei1064 – 1065Cleavage; by 3CLSP2
Sitei1268 – 1269Cleavage; by 3CLSP; in major pathway2
Sitei1430 – 1431Cleavage; by 3CLSP; in minor pathway2
Sitei1452 – 1453Cleavage; by 3CLSP; in minor pathway2
Sitei1575 – 1576Cleavage; by 3CLSP2
Sitei1677 – 1678Cleavage; by 3CLSP2
Sitei2370 – 2371Cleavage; by 3CLSP2
Sitei2837 – 2838Cleavage; by 3CLSP2
Sitei3056 – 3057Cleavage; by 3CLSP2

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

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

Structurei

Secondary structure

13175
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi270 – 277Combined sources8
Turni278 – 280Combined sources3
Beta strandi283 – 286Combined sources4
Helixi290 – 292Combined sources3
Helixi296 – 305Combined sources10
Beta strandi309 – 312Combined sources4
Beta strandi323 – 329Combined sources7
Beta strandi332 – 337Combined sources6
Helixi347 – 351Combined sources5
Helixi369 – 379Combined sources11
Turni380 – 382Combined sources3
Beta strandi383 – 386Combined sources4
Beta strandi1076 – 1092Combined sources17
Beta strandi1095 – 1101Combined sources7
Helixi1102 – 1105Combined sources4
Beta strandi1110 – 1115Combined sources6
Beta strandi1118 – 1123Combined sources6
Beta strandi1125 – 1127Combined sources3
Beta strandi1130 – 1135Combined sources6
Turni1137 – 1139Combined sources3
Beta strandi1154 – 1161Combined sources8
Beta strandi1164 – 1170Combined sources7
Helixi1181 – 1183Combined sources3
Beta strandi1187 – 1190Combined sources4
Beta strandi1193 – 1202Combined sources10
Helixi1203 – 1205Combined sources3
Beta strandi1206 – 1210Combined sources5
Beta strandi1216 – 1220Combined sources5
Helixi1224 – 1228Combined sources5
Beta strandi1233 – 1237Combined sources5
Beta strandi1250 – 1254Combined sources5
Helixi1255 – 1262Combined sources8
Turni1454 – 1459Combined sources6
Helixi1463 – 1474Combined sources12
Beta strandi1476 – 1480Combined sources5
Beta strandi1483 – 1486Combined sources4
Helixi1490 – 1506Combined sources17
Helixi1510 – 1520Combined sources11
Turni1521 – 1524Combined sources4
Beta strandi1533 – 1539Combined sources7
Beta strandi1545 – 1548Combined sources4
Beta strandi1551 – 1560Combined sources10
Beta strandi1565 – 1573Combined sources9
Turni2375 – 2377Combined sources3
Beta strandi2382 – 2385Combined sources4
Turni2393 – 2395Combined sources3
Helixi2396 – 2399Combined sources4
Beta strandi2400 – 2403Combined sources4
Beta strandi2405 – 2409Combined sources5
Helixi2416 – 2418Combined sources3
Beta strandi2419 – 2423Combined sources5
Turni2424 – 2428Combined sources5
Helixi2440 – 2451Combined sources12
Beta strandi2457 – 2462Combined sources6
Beta strandi2465 – 2468Combined sources4
Beta strandi2470 – 2475Combined sources6
Beta strandi2478 – 2483Combined sources6
Beta strandi2488 – 2494Combined sources7
Beta strandi2496 – 2503Combined sources8
Helixi2513 – 2521Combined sources9
Beta strandi2524 – 2527Combined sources4
Helixi2534 – 2544Combined sources11
Beta strandi2549 – 2552Combined sources4
Helixi2556 – 2568Combined sources13
Beta strandi2591 – 2596Combined sources6
Beta strandi2605 – 2609Combined sources5
Turni2610 – 2614Combined sources5
Helixi2617 – 2626Combined sources10
Beta strandi2630 – 2633Combined sources4
Turni2648 – 2651Combined sources4
Helixi2652 – 2654Combined sources3
Beta strandi2655 – 2657Combined sources3
Beta strandi2665 – 2667Combined sources3
Helixi2669 – 2674Combined sources6
Turni2675 – 2678Combined sources4
Beta strandi2690 – 2693Combined sources4
Beta strandi2702 – 2708Combined sources7
Helixi2709 – 2711Combined sources3
Beta strandi2717 – 2719Combined sources3
Helixi2720 – 2722Combined sources3
Beta strandi2727 – 2733Combined sources7
Beta strandi2736 – 2738Combined sources3
Helixi2742 – 2748Combined sources7
Beta strandi2750 – 2759Combined sources10
Helixi2765 – 2768Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5HBZX-ray3.10A/B/C/D/E/F2838-3056[»]
5HC1X-ray3.10A/B/C/D2838-3056[»]
ProteinModelPortaliP19811.
SMRiP19811.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19811.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini66 – 156Peptidase C31PROSITE-ProRule annotationAdd BLAST91
Domaini157 – 260Peptidase C32PROSITE-ProRule annotationAdd BLAST104
Domaini261 – 360Peptidase C33PROSITE-ProRule annotationAdd BLAST100
Domaini1065 – 1268Peptidase S32PROSITE-ProRule annotationAdd BLAST204
Domaini2116 – 2251RdRp catalyticPROSITE-ProRule annotationAdd BLAST136
Domaini2371 – 2438AV ZBDPROSITE-ProRule annotationAdd BLAST68
Domaini2496 – 2661(+)RNA virus helicase ATP-bindingAdd BLAST166
Domaini2662 – 2793(+)RNA virus helicase C-terminalAdd BLAST132

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni261 – 339OTU-likeAdd BLAST79
Regioni530 – 645HD1Add BLAST116
Regioni829 – 997HD2Add BLAST169
Regioni1291 – 1405HD3Add BLAST115

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi389 – 440Pro-richAdd BLAST52

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 AV ZBD (arterivirus zinc-binding) domain.PROSITE-ProRule annotation
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)DescriptionActionsGraphical viewLength
Zinc fingeri25 – 44C4-type; atypicalAdd BLAST20

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.30.40.20. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR031932. Arteri_nsp7a.
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.
IPR032786. Nsp3.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
[Graphical view]
PfamiPF16749. Arteri_nsp7a. 1 hit.
PF12581. DUF3756. 1 hit.
PF14755. ER-remodelling. 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.
PS51493. AV_NSP4_PRO. 1 hit.
PS51539. AV_PCP_ALPHA. 1 hit.
PS51540. AV_PCP_BETA. 1 hit.
PS51652. AV_ZBD. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0328871728 – 3175Missing in isoform Replicase polyprotein 1a. CuratedAdd BLAST1448

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.
KEGGivg:921339.

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.
PIRiA39925. RRWVEV.
RefSeqiNP_127506.1. NC_002532.2.
NP_127507.1. NC_002532.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5HBZX-ray3.10A/B/C/D/E/F2838-3056[»]
5HC1X-ray3.10A/B/C/D2838-3056[»]
ProteinModelPortaliP19811.
SMRiP19811.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC33.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi921339.
KEGGivg:921339.

Enzyme and pathway databases

BRENDAi3.4.21.114. 6985.

Miscellaneous databases

EvolutionaryTraceiP19811.

Family and domain databases

Gene3Di3.30.40.20. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR031932. Arteri_nsp7a.
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.
IPR032786. Nsp3.
IPR027417. P-loop_NTPase.
IPR009003. Peptidase_S1_PA.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
[Graphical view]
PfamiPF16749. Arteri_nsp7a. 1 hit.
PF12581. DUF3756. 1 hit.
PF14755. ER-remodelling. 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.
PS51493. AV_NSP4_PRO. 1 hit.
PS51539. AV_PCP_ALPHA. 1 hit.
PS51540. AV_PCP_BETA. 1 hit.
PS51652. AV_ZBD. 1 hit.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 148 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.