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P0C6W1

- R1AB_BC133

UniProt

P0C6W1 - R1AB_BC133

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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Bat coronavirus 133/2005 (BtCoV) (BtCoV/133/2005)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi

Functioni

The replicase polyprotein of coronaviruses 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.By similarity
Host translation inhibitor nsp1: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.By similarity1 Publication
Non-structural protein 2: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.By similarity
Papain-like proteinase: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.By similarity
Non-structural protein 4: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.By similarity
Proteinase 3CL-PRO: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).By similarityPROSITE-ProRule annotation
Non-structural protein 6: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.By similarity
Non-structural protein 7: Forms an hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.By similarity
Non-structural protein 8: Forms an hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.By similarity
Non-structural protein 9: May participate in viral replication by acting as a ssRNA-binding protein.By similarity
Non-structural protein 10: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.By similarity
RNA-directed RNA polymerase: Responsible for replication and transcription of the viral RNA genome.By similarity
Helicase: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.By similarity
Guanine-N7 methyltransferase: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity.By similarity
Uridylate-specific endoribonuclease: Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.By similarity
2'-O-methyltransferase: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.
TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
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
Sitei195 – 1962CleavageSequence Analysis
Sitei847 – 8482Cleavage; by PL-PROSequence Analysis
Active sitei1641 – 16411For PL-PRO activityPROSITE-ProRule annotation
Active sitei1807 – 18071For PL-PRO activityPROSITE-ProRule annotation
Sitei2791 – 27922Cleavage; by PL-PROSequence Analysis
Sitei3298 – 32992Cleavage; by 3CL-PROSequence Analysis
Active sitei3339 – 33391For 3CL-PRO activityPROSITE-ProRule annotation
Active sitei3446 – 34461For 3CL-PRO activityPROSITE-ProRule annotation
Sitei3604 – 36052Cleavage; by 3CL-PROSequence Analysis
Sitei3896 – 38972Cleavage; by 3CL-PROSequence Analysis
Sitei3979 – 39802Cleavage; by 3CL-PROSequence Analysis
Sitei4178 – 41792Cleavage; by 3CL-PROSequence Analysis
Sitei4288 – 42892Cleavage; by 3CL-PROSequence Analysis
Sitei4427 – 44282Cleavage; by 3CL-PROSequence Analysis
Sitei5361 – 53622Cleavage; by 3CL-PROSequence Analysis
Sitei5959 – 59602Cleavage; by 3CL-PROSequence Analysis
Sitei6482 – 64832Cleavage; by 3CL-PROSequence Analysis
Sitei6824 – 68252Cleavage; by 3CL-PROSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1721 – 175838C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4362 – 437817By similarityAdd
BLAST
Zinc fingeri4404 – 441714By similarityAdd
BLAST
Nucleotide bindingi5643 – 56508ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. endonuclease activity Source: UniProtKB-KW
  4. exoribonuclease activity, producing 5'-phosphomonoesters Source: InterPro
  5. helicase activity Source: UniProtKB-KW
  6. methyltransferase activity Source: InterPro
  7. omega peptidase activity Source: InterPro
  8. RNA binding Source: UniProtKB-KW
  9. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  10. zinc ion binding Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Endonuclease, Exonuclease, Helicase, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

Keywords - Biological processi

Activation of host autophagy by virus, Decay of host mRNAs by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, 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, Inhibition of host NF-kappa-B by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion, Viral RNA replication

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Replicase polyprotein 1ab
Short name:
pp1ab
Alternative name(s):
ORF1ab polyprotein
Cleaved into the following 15 chains:
Alternative name(s):
Leader protein
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p65 homolog
Papain-like proteinase (EC:3.4.19.12, EC:3.4.22.69)
Short name:
PL-PRO
Alternative name(s):
Non-structural protein 3
Short name:
nsp3
Non-structural protein 4
Short name:
nsp4
3C-like proteinase (EC:3.4.22.-)
Short name:
3CL-PRO
Short name:
3CLp
Alternative name(s):
nsp5
Non-structural protein 6
Short name:
nsp6
Non-structural protein 7
Short name:
nsp7
Non-structural protein 8
Short name:
nsp8
Non-structural protein 9
Short name:
nsp9
Non-structural protein 10
Short name:
nsp10
Alternative name(s):
Growth factor-like peptide
Short name:
GFL
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
Pol
Short name:
RdRp
Alternative name(s):
nsp12
Helicase (EC:3.6.4.12, EC:3.6.4.13)
Short name:
Hel
Alternative name(s):
nsp13
Alternative name(s):
nsp14
Alternative name(s):
NendoU
nsp15
Alternative name(s):
nsp16
Gene namesi
Name:rep
ORF Names:1a-1b
OrganismiBat coronavirus 133/2005 (BtCoV) (BtCoV/133/2005)
Taxonomic identifieri389230 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirusunclassified Betacoronavirus
Virus hostiTylonycteris pachypus (Lesser bamboo bat) [TaxID: 258959]
ProteomesiUP000007449: Genome

Subcellular locationi

Chain Papain-like proteinase : Host membrane; Multi-pass membrane protein. Host cytoplasm By similarity
Chain Non-structural protein 4 : Host membrane; Multi-pass membrane protein. Host cytoplasm
Note: Localizes in virally-induced cytoplasmic double-membrane vesicles.By similarity
Chain Non-structural protein 7 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Non-structural protein 8 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Non-structural protein 9 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Non-structural protein 10 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Helicase : Host endoplasmic reticulum-Golgi intermediate compartment Curated
Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195Host translation inhibitor nsp1By similarityPRO_0000290273Add
BLAST
Chaini196 – 847652Non-structural protein 2By similarityPRO_0000290274Add
BLAST
Chaini848 – 27911944Papain-like proteinaseBy similarityPRO_0000290275Add
BLAST
Chaini2792 – 3298507Non-structural protein 4By similarityPRO_0000290276Add
BLAST
Chaini3299 – 36043063C-like proteinaseBy similarityPRO_0000290277Add
BLAST
Chaini3605 – 3896292Non-structural protein 6By similarityPRO_0000290278Add
BLAST
Chaini3897 – 397983Non-structural protein 7By similarityPRO_0000290279Add
BLAST
Chaini3980 – 4178199Non-structural protein 8By similarityPRO_0000290280Add
BLAST
Chaini4179 – 4288110Non-structural protein 9By similarityPRO_0000290281Add
BLAST
Chaini4289 – 4427139Non-structural protein 10By similarityPRO_0000290282Add
BLAST
Chaini4428 – 5361934RNA-directed RNA polymeraseBy similarityPRO_0000290283Add
BLAST
Chaini5362 – 5959598HelicaseBy similarityPRO_0000290284Add
BLAST
Chaini5960 – 6482523Guanine-N7 methyltransferaseBy similarityPRO_0000290285Add
BLAST
Chaini6483 – 6824342Uridylate-specific endoribonucleaseBy similarityPRO_0000290286Add
BLAST
Chaini6825 – 71263022'-O-methyltransferaseBy similarityPRO_0000290287Add
BLAST

Post-translational modificationi

Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity).By similarity

Proteomic databases

PRIDEiP0C6W1.

Interactioni

Subunit structurei

Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the homodimer shows catalytic activity. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure. Nsp9 is a dimer. Nsp10 forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1.By similarity

Structurei

3D structure databases

ProteinModelPortaliP0C6W1.
SMRiP0C6W1. Positions 3896-3979, 4228-4288, 4298-4418.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2119 – 213921HelicalSequence AnalysisAdd
BLAST
Transmembranei2152 – 217221HelicalSequence AnalysisAdd
BLAST
Transmembranei2229 – 224921HelicalSequence AnalysisAdd
BLAST
Transmembranei2333 – 235321HelicalSequence AnalysisAdd
BLAST
Transmembranei2357 – 237721HelicalSequence AnalysisAdd
BLAST
Transmembranei2382 – 240221HelicalSequence AnalysisAdd
BLAST
Transmembranei2807 – 282721HelicalSequence AnalysisAdd
BLAST
Transmembranei3079 – 309921HelicalSequence AnalysisAdd
BLAST
Transmembranei3112 – 313221HelicalSequence AnalysisAdd
BLAST
Transmembranei3156 – 317621HelicalSequence AnalysisAdd
BLAST
Transmembranei3610 – 363021HelicalSequence AnalysisAdd
BLAST
Transmembranei3644 – 366421HelicalSequence AnalysisAdd
BLAST
Transmembranei3669 – 368921HelicalSequence AnalysisAdd
BLAST
Transmembranei3714 – 373421HelicalSequence AnalysisAdd
BLAST
Transmembranei3742 – 376221HelicalSequence AnalysisAdd
BLAST
Transmembranei3791 – 381121HelicalSequence AnalysisAdd
BLAST
Transmembranei3815 – 383521HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1159 – 1328170MacroPROSITE-ProRule annotationAdd
BLAST
Domaini1600 – 1871272Peptidase C16PROSITE-ProRule annotationAdd
BLAST
Domaini3299 – 3604306Peptidase C30PROSITE-ProRule annotationAdd
BLAST
Domaini5041 – 5203163RdRp catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini5362 – 544584CV MBDAdd
BLAST
Domaini5618 – 5799182(+)RNA virus helicase ATP-bindingAdd
BLAST
Domaini5800 – 5974175(+)RNA virus helicase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2119 – 2402284HD1By similarityAdd
BLAST
Regioni2807 – 3176370HD2By similarityAdd
BLAST
Regioni3610 – 3835226HD3By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi960 – 1059100Glu-richAdd
BLAST
Compositional biasi5366 – 539126Cys-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.By similarity

Sequence similaritiesi

Contains 1 Macro domain.PROSITE-ProRule annotation
Contains 1 peptidase C16 domain.PROSITE-ProRule annotation
Contains 1 peptidase C30 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1721 – 175838C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4362 – 437817By similarityAdd
BLAST
Zinc fingeri4404 – 441714By similarityAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR009466. NSP11.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases-like.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF06478. Corona_RPol_N. 1 hit.
PF01661. Macro. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF00680. RdRP_1. 1 hit.
PF11633. SUD-M. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view]
SUPFAMiSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51653. CV_MBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 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: P0C6W1-1) [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.

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        10         20         30         40         50
MLSKAGVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTED MASKLTPWFE
60 70 80 90 100
DGETAFNQVS SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS
110 120 130 140 150
KHFLVNQLAY KDHVGAAMMR TTLNVKPLGM FFPYDSSLET GEHTFLLRKN
160 170 180 190 200
GLGGQLFRER PWDRKETPYV EILDDLEADP TGKYSQNLLK KLIGGDCIPV
210 220 230 240 250
DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS DRFIVLNKKL
260 270 280 290 300
YRVVWNVTRR NVPYSKQTAF TVVSVIQCDD KESVPEHTFT IGSQILMVSP
310 320 330 340 350
LKATNNKNFN LKQRLLHTFY GKEAVQQPGY IYHSAYVDCN ACGRGTWCTG
360 370 380 390 400
NAIQGFACDC GANYSANDVD LQSSGLVPKN ALFLANCPCA NNGACSHNAA
410 420 430 440 450
QVYSILDGKA CVEVGGKSFT LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR
460 470 480 490 500
IGDAIFTGCT GTWDKVVETA NLFLEKAQHS LNFCQQFALT EVVLAILSGT
510 520 530 540 550
TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI NIGANGVCNA
560 570 580 590 600
TINAPFIAFT GLGESFKKVA AIPWKICSNL KSALDYYCSN IMFRVFPYDI
610 620 630 640 650
PCDVNDFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SNACQTALSS
660 670 680 690 700
FLNACVAASR ATAGFISDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ
710 720 730 740 750
QVLDIMSKAM KLLHTNVSWA GTKLSAIIYE GREALLFNSG TYFCLSTKAK
760 770 780 790 800
TLQDQMNLVL PGDYNKKTLG ILDPVPNADT IDVTANSTVV DVVHGQLEPT
810 820 830 840 850
NEHGPSMIVG NYVLVSDKLF VRTDDEEFYP LCINGKVVST LFRLKGGMPS
860 870 880 890 900
KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
910 920 930 940 950
DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN
960 970 980 990 1000
MTFSINPVED VEEVEEFIED DYLSDELPIA DDEEAWTRAV EEVMPLDDIL
1010 1020 1030 1040 1050
VAEIELEEDL PLETALESVE AEVGESISDE LCVVETAKAQ EPSVESTDST
1060 1070 1080 1090 1100
PSTSTVVSEN DLSVKPMSRV AETGDVLEVE TAVVGGPVSD VTASVVTNDI
1110 1120 1130 1140 1150
VSVEQAQQCG VSSLPIQDEA SENQVHQVPD LQCTSETKVE IVQPRQDLRP
1160 1170 1180 1190 1200
RRLRKSKVDL SKYKHTVINN SVTLVLGDAI QIASLLPKCV LVNAANRHLK
1210 1220 1230 1240 1250
HGGGIAGAIN KASGGDVQEE SDEYISNSGP LHVGDSVLLK GYGLADAILR
1260 1270 1280 1290 1300
VVGPDARNNE DAALLKRCYK TFNKHTIVVT PLISSGIFSV DPKVSFEYLL
1310 1320 1330 1340 1350
ANVTTTTYVV VNNEDIYNTL ATPSKPDGLV YSFEGWRGTV RTAKNYGFTC
1360 1370 1380 1390 1400
FICTEYSANV KFLRTKGVDT TKKIQTVDGV SYYLYSARDA LTDVIAAANG
1410 1420 1430 1440 1450
CPGICAMPFG YVTHGLDLAQ SGNYVRQVKV PYVCLLASKE QIPIMNSDVA
1460 1470 1480 1490 1500
IQTPETAFIN NVTSNGGYHS WHLVSGDLIV KDVCYKKLLH WSGQTICYAD
1510 1520 1530 1540 1550
NKFYVVKNDV ALPFSDLEAC RAYLTSRAAQ QVNIEVLVTI DGVNFRTVIL
1560 1570 1580 1590 1600
NDATTFRKQL GATFYKGVDI SDALPTVKMG GESLFVADNL SESEEVVLKE
1610 1620 1630 1640 1650
YYGTSDVTFL QRYYSLQPLV QQWKFVVHDG VKSLKLSNYN CYINATIMMI
1660 1670 1680 1690 1700
DMLHDIKFVV PALQNAYLRY KGGDPYDFLA LIMAYGDCTF DNPDDEAKLL
1710 1720 1730 1740 1750
HTLLAKAELT VSAKMVWREW CTVCGIRDIE YTGMRACVYA GVNSMEELQS
1760 1770 1780 1790 1800
VFNETCVCGS VKHRQLVEHS TPWLLVSGLN EVKVSTSTDP VYRAFNVFQG
1810 1820 1830 1840 1850
VETSVGHYVH VRVKDGLFYK YDSGSLTKTS DMKCKMTSVW YPKVRYTADC
1860 1870 1880 1890 1900
NVVVYDLDGV TKVEVNPDLS NYYMKDGKYY TSKPTIKYSP ATILPGSVYS
1910 1920 1930 1940 1950
NSCLVGVDGT PGSDTISKFF NDLLGFDETK PISKKLTYSL LPNEDGDVLL
1960 1970 1980 1990 2000
SEFNNYNPVY KKGVMLKGKP ILWVNNGVCD SALNKPNRAS LRQLYDVAPI
2010 2020 2030 2040 2050
VLDNKYTVLQ DNTSQLIEPN VPVVEDVSIT TRKLIEVKCK GLNKPFVKGN
2060 2070 2080 2090 2100
FSFVNDPNGV TVVDTLGLTE LRALYVDINT RYIVLRDNNW SSLFKLHTVE
2110 2120 2130 2140 2150
SGDLQIVANG GSVTRRARVL LGASSLFASF AKITVTATTA ACKTAGRSFC
2160 2170 2180 2190 2200
KFVVNYGVLQ NMFLFLKMLF FLPFNYLWPK KQPTVDVGVS GLRTAGVVTT
2210 2220 2230 2240 2250
NIVKQCGTAA YYMLLGKFKR VDWKATLRLF LLLCTTILLL SSIYHLVIFN
2260 2270 2280 2290 2300
QVLSSDVMLE DATGILAMYK EVRSYLGIRT LCDGLAVEYR NTSFDVVDFC
2310 2320 2330 2340 2350
SNRSVLCQWC LIGQDSLTRY SALQMLQTHI TSYVLNIDWI WFALEFFLAY
2360 2370 2380 2390 2400
VLYTSSFNVL LLVVTAQYFF AYTSAFVNWR AYNYIVSGLF FLVTHIPLHG
2410 2420 2430 2440 2450
LVRVYNFLAC LWFLRKFYSH VINGCKDTAC LLCYKRNRLT RVEASTIVCG
2460 2470 2480 2490 2500
TKRTFYIAAN GGTSYCCKHN WNCVECDTAG VGNTFICTEV ANDLTTTLRR
2510 2520 2530 2540 2550
LIKPTDQSHY YVDSVVVKDA VVELHYNRDG SSCYERYPLC YFTNLEKLKF
2560 2570 2580 2590 2600
KEVCKTPTGI PEHNFLIYDT NDRGQENLAR SACVYYSQVL CKPMLLVDVN
2610 2620 2630 2640 2650
LVTTVGDSRE IAIKMLDSFI NSFISLFSVS RDKLEKLINT ARDCVRRGDD
2660 2670 2680 2690 2700
FQTVLKTFTD AARGHAGVES DVETTMVVDA LQYAHKNDIQ LTTECYNNYV
2710 2720 2730 2740 2750
PGYIKPDSIN TLDLGCLIDL KAASVNQTSM RNANGACVWN SGDYMKLSDS
2760 2770 2780 2790 2800
FKRQIRIACR KCNIPFRLTT SKLRAADNIL SVKFSATKIV GGAPSWLLRV
2810 2820 2830 2840 2850
RDLTVKGYCI LTLFVFTVAV LSWFCLPSYS IATVNFNDDR ILTYKVIENG
2860 2870 2880 2890 2900
IVRDIAPNDA CFANKYGHFS KWFNENHGGV YRNSVDCPIT IAVIAGVAGA
2910 2920 2930 2940 2950
RVANVPATLA WVGRQIVLFV SRVFANTNVC FTPTNEIPYD TFSDSGCVLS
2960 2970 2980 2990 3000
SECTLFRDAE GNLNPFCYDP TVLPGASSYA DMKPHVRYDM YDSDMYIKFP
3010 3020 3030 3040 3050
EVIFESTLRI TKTLATQYCR FGSCEESAAG VCISTNGSWA LYNQNYSTRP
3060 3070 3080 3090 3100
GIYCGDDYFD IVRRLAVSLF QPVTYFQLST SLAMGLVLCV FLTAAFYYIN
3110 3120 3130 3140 3150
KVKRALADYT QCAVVAVVAA LLNSLCLCFI VANPLLVAPY TAMYYYATFY
3160 3170 3180 3190 3200
LTGEPAFIMH ISWYVMFGTV VPIWMLASYT VGVMLRHLFW VLAYFSKKHV
3210 3220 3230 3240 3250
DVFTDGKLNC SFQDAASNIF VIGKDTYVAL RNAITQDSFV RYLSLFNKYK
3260 3270 3280 3290 3300
YYSGAMDTAS YREACAAHLC KALQTYSETG SDILYQPPNC SVTSSVLQSG
3310 3320 3330 3340 3350
LVKMSAPSGA VENCIVQVTC GSMTLNGLWL DNTVWCPRHI MCPADQLTDP
3360 3370 3380 3390 3400
NYDALLISKT NHSFIVQKHI GAQANLRVVA HSMVGVLLKL TVDVANPSTP
3410 3420 3430 3440 3450
AYTFSTVKPG ASFSVLACYN GKPTGVFTVN LRHNSTIKGS FLCGSCGSVG
3460 3470 3480 3490 3500
YTENGGVLNF VYMHQMELSN GTHTGSSFDG VMYGAFEDKQ THQLQLTDKY
3510 3520 3530 3540 3550
CTINVVAWLY AAVLNGCKWF VKPTRVGIVT YNEWALSNQF TEFVGTQSID
3560 3570 3580 3590 3600
MLAHRTGVSV EQMLAAIQSL HAGFQGKTIL GQSTLEDEFT PDDVNMQVMG
3610 3620 3630 3640 3650
VVMQSGVKRI SYGFMHWLMS TLVLAYVSVM QLTKFTMWTY LFETIPTQMT
3660 3670 3680 3690 3700
PLLFGFMACV MFTVKHKHTF LSLFLLPVAL CLTYANIVYE PQTLVSSTLI
3710 3720 3730 3740 3750
AVANWLTPTS VYMRTTHLDF GLYISLSFVL AIIVRRLYRP SMSNLALALC
3760 3770 3780 3790 3800
SGVMWFYTYV IGDHSSPITY LMFITTLTSD YTITVFATVN LAKFISGLVF
3810 3820 3830 3840 3850
LYAPHLGFIL PEVKLVLLIY LCLGYMCTMY FGVFSLLNLK LRVPLGVYDY
3860 3870 3880 3890 3900
SVSTQEFRFL TGNGLHAPRN SWEALILNFK LLGIGGTPCI KVATVQSKLT
3910 3920 3930 3940 3950
DLKCTSVVLL TVLQQLHLES NSKAWSYCVK LHNEILAAVD PTEAFERFVC
3960 3970 3980 3990 4000
LFATLMSFSA NVDLDALAND LFENSSVLQA TLTEFSHLAT YAELETAQSS
4010 4020 4030 4040 4050
YQKALNSGDA SPQVLKALQK AVNVAKNAYE KDKAVARKLE RMAEQAMTSM
4060 4070 4080 4090 4100
YKQARAEDKK AKIVSAMQTM LFGMIKKLDN DVLNGVIANA RNGCVPLSIV
4110 4120 4130 4140 4150
PLCASNKLRV VIPDISVWNK VVNWPSVSYA GSLWDVTVIN NVDNEVVKPT
4160 4170 4180 4190 4200
DVVETNESLT WPLVIECSRA SSSAVKLQNN EIHPKGLKTM VVTAGIDQVN
4210 4220 4230 4240 4250
CSSSAVAYYE PVQGHRMVMG LLSENAHLKW AKVEGKDGFI NIELQPPCKF
4260 4270 4280 4290 4300
LIAGPKGPEI RYLYFVKNLN NLHRGQLLGH IAATVRLQAG ANTEFASNST
4310 4320 4330 4340 4350
VLTLVAFAVD PAKAYLDYVG SGGTPLSNYV KMLAPKTGTG VAISVKPEAT
4360 4370 4380 4390 4400
ADQETYGGAS VCLYCRAHIE HPDVSGVCKY KTRFVQIPAH VRDPVGFLLK
4410 4420 4430 4440 4450
NVPCNVCQYW VGYGCNCDAL RNNTVPQSKD TNFLNRVRGS SVNARLEPCS
4460 4470 4480 4490 4500
SGLTTDVVYR AFDICNFKAR VAGIGKYYKT NTCRFVQVDD EGHKLDSYFI
4510 4520 4530 4540 4550
VKRHTMSNYE LEKRCYDLLK DCDAVAIHDF FIFDVDKTKT PHIVRQSLTE
4560 4570 4580 4590 4600
YTMMDLVYAL RHFDQNNCEV LKSILVKYGC CEQSYFDNKL WFDFVENPSV
4610 4620 4630 4640 4650
IGVYHKLGER IRQAMLNTVK MCDHMVKSGL VGVLTLDNQD LNGKWYDFGD
4660 4670 4680 4690 4700
FVITQPGAGV AIVDSYYSYL MPVLSMTNCL AAETHKDCDF NKPLIEWLLL
4710 4720 4730 4740 4750
EYDYTDYKIG LFNKYFKHWD QTYHPNCVNC GDDRCILHCA NFNVLFSMVL
4760 4770 4780 4790 4800
PNTSFGPIVR KIFVDGVPFI VSCGYHYKEL GLVMNMDVNI HRHRLALKEL
4810 4820 4830 4840 4850
MMYAADPAMH IASASALWDL RTPCFSVAAL TTGLTFQTVR PGNFNKDFYD
4860 4870 4880 4890 4900
FVVSRGFFKE GSSVTLKHFF FAQDGHAAIT DYSYYAYNLP TMVDIKQMLF
4910 4920 4930 4940 4950
CMEVVDKYFD IYDGGCLNAS EVIVNNLDKS AGHPFNKFGK ARVYYESMSY
4960 4970 4980 4990 5000
QEQDELFAVT KRNVLPTITQ MNLKYAISAK NRARTVAGVS ILSTMTNRQY
5010 5020 5030 5040 5050
HQKMLKSMAA TRGATCVIGT TKFYGGWDFM LKTLYKDVES PHLMGWDYPK
5060 5070 5080 5090 5100
CDRAMPNMCR ILASLILARK HSTCCTNSDR FYRLANECAQ VLSEYVLCGG
5110 5120 5130 5140 5150
GYYVKPGGTS SGDATTAYAN SVFNILQATT ANVSALMSAN GNTIIDREIK
5160 5170 5180 5190 5200
DMQFDLYINV YRKVVPDPKF VDKYYAFLNK HFSMMILSDD GVVCYNSDYA
5210 5220 5230 5240 5250
AKGYVASIQN FKETLYYQNN VFMSEAKCWV ETNLEKGPHE FCSQHTLYIK
5260 5270 5280 5290 5300
DGDDGYFLPY PDPSRILSAG CFVDDIVKTD GTVMMERYVS LAIDAYPLTK
5310 5320 5330 5340 5350
HDDTEYQNVF WVYLQYIEKL YKDLTGHMLD SYSVMLCGDD SAKFWEEGFY
5360 5370 5380 5390 5400
RDLYSSPTTL QAVGSCVVCH SQTSLRCGTC IRRPFLCCKC CYDHVIATTH
5410 5420 5430 5440 5450
KMVLSVSPYV CNAPGCDVSD VTKLYLGGMS YYCNDHRPVC SFPLCANGLV
5460 5470 5480 5490 5500
FGLYKNMCTG SSSIMEFNRL ATCDWSDSGD YTLANTTTEP LKLFAAETLR
5510 5520 5530 5540 5550
ATEEASKQSY AIATIKEIVG ERELILVWEV GKSKPPLNRN YVFTGYHLTK
5560 5570 5580 5590 5600
NSKVQLGEYV FERIDYSDAV SYKSSTTYKL AVGDIFVLTS HSVATLSAPT
5610 5620 5630 5640 5650
IVNQERYLKI TGIYPTITVP EEFANHVVNF QKAGFSKYVT VQGPPGTGKS
5660 5670 5680 5690 5700
HFAIGLAIYY PTARIVYTAC SHAAVDALCA KAFKYLNIAK CSRIIPAKAR
5710 5720 5730 5740 5750
VECYDRFKVN DTNAQYLFST VNALPEISVD ILVVDEVSMC TNYDLSIINS
5760 5770 5780 5790 5800
RVKAKHIVYV GDPAQLPAPR TLLTRGTLEP ENFNSVTRLM CNLGPDIFLS
5810 5820 5830 5840 5850
VCYRCPKEIV NTVSALVYNN KLSAKKDASG QCFKILFKGS VTHDASSAIN
5860 5870 5880 5890 5900
RPQLNFVKTF IAANPNWSKA VFISPYNSQN AVARSMLGLT TQTVDSSQGS
5910 5920 5930 5940 5950
EYPYVIFCQT ADTAHANNLN RFNVAVTRAQ KGILCVMTSQ VLFDSLEFAE
5960 5970 5980 5990 6000
LSLNNYKLQS QIVTGLFKDC SREDVGLPPA YAPTYLSVDA KYKTTDELCV
6010 6020 6030 6040 6050
NLNITPNVTY SRVISRMGFK LDATIPGYPK LFITRDEAIR QVRSWIGFDV
6060 6070 6080 6090 6100
EGAHASRNAC GTNVPLQLGF STGVNFVVQP VGVVDTEWGS MLTTISARPP
6110 6120 6130 6140 6150
PGEQFKHLVP LMNKGATWPI VRRRIVQMLS DTLDKLSDYC TFVCWAHGFE
6160 6170 6180 6190 6200
LTSASYFCKI GKEQRCCMCS RRASTFSSPL QSYACWSHSS GYDYVYNPFF
6210 6220 6230 6240 6250
VDVQQWGYVG NLATNHDRYC GIHAGAHVAS SDAIMTRCLA IYDCFIERVD
6260 6270 6280 6290 6300
WDVTYPYISH EQKLNSCCRT VERNVVRSAV LSGKFDKIYD IGNPKGIPII
6310 6320 6330 6340 6350
SEPVEWHFYD AQPLSNKVKK LFYTDDVAKQ FEDGLCLFWN CNVSKYPSNA
6360 6370 6380 6390 6400
VVCRFDTRVH SEFNLPGCNG GSLYVNKHAF HTPAYDINAF RDLKPLPFFY
6410 6420 6430 6440 6450
YSTTPCEVHG SGNMLEDIDY VPLKSAVCIT ACNLGGAVCR KHAAEYRDYM
6460 6470 6480 6490 6500
EAYNIVSAAG FRLWVYKTFD IYNLWSTFVK VQGLENIAFN VIKQGHFTGV
6510 6520 6530 6540 6550
DGELPVAVVN DKIFTKNGTD DVCIFKNETA LPTNVAFELY AKRAVRSHPD
6560 6570 6580 6590 6600
LNLLRNLEVD VCYNFVLWDY DRNNIYGTTT IGVCKYTDID VNPNLNMCFD
6610 6620 6630 6640 6650
IRDKGSLERF MSMPNGVLIS DRKIKNYPCI IGPKHAYFNG AILRNIDAKQ
6660 6670 6680 6690 6700
PITFYLYKKV NNEFVSFSDT FYTCGRTVND FTALTPMEED FLVLDSDVFI
6710 6720 6730 6740 6750
KKYSLEDYAF EHVVYGDFSH TTLGGLHLLI GLYKKMRDGH ILMEEMLKDR
6760 6770 6780 6790 6800
ATVHNYFITD SNTASYKAVC SVIDLRLDDF VNIIKEMDLD VVSKVVKVPI
6810 6820 6830 6840 6850
DLTMIEFMLW CKDGKVQTFY PRLQATNDWK PGLTMPSLFK VQQMNLEPCL
6860 6870 6880 6890 6900
LANYKQSIPM PNGVHMNVAK YMQLCQYLNT CTLAVPANMR VIHFGAGCEK
6910 6920 6930 6940 6950
GVAPGTSVLR QWLPLDAVLI DNDLNEFVSD ADITIFGDCV TVHVGQQVDL
6960 6970 6980 6990 7000
LISDMYDPCT KAVGEVNQTK ALFFVYLCNF IKNNLALGGS VAIKITEHSW
7010 7020 7030 7040 7050
SADLYKIMGR FAYWTVFCTN ANASSSEGFL IGINFLGELK EEIDGNVMHA
7060 7070 7080 7090 7100
NYIFWRNSTP MNLSTYSLFD LSRFPLKLKG TPVLQLKESQ INELVISLLS
7110 7120
QGKLLIRDND TLNVSTDVLV NFRKRL

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

Length:7,126
Mass (Da):795,781
Last modified:June 10, 2008 - v1
Checksum:i23A0EB77D0CFD96F
GO
Isoform Replicase polyprotein 1a (identifier: P0C6F7-1) [UniParc]FASTAAdd to Basket

Also known as: pp1a, ORF1a polyprotein

The sequence of this isoform can be found in the external entry P0C6F7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Length:4,441
Mass (Da):492,464
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ648794 Genomic RNA. Translation: ABG47051.1.
RefSeqiYP_729202.1. NC_008315.1. [P0C6W1-1]

Genome annotation databases

GeneIDi5142284.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ648794 Genomic RNA. Translation: ABG47051.1 .
RefSeqi YP_729202.1. NC_008315.1. [P0C6W1-1 ]

3D structure databases

ProteinModelPortali P0C6W1.
SMRi P0C6W1. Positions 3896-3979, 4228-4288, 4298-4418.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P0C6W1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5142284.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR009466. NSP11.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases-like.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view ]
Pfami PF06478. Corona_RPol_N. 1 hit.
PF01661. Macro. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF00680. RdRP_1. 1 hit.
PF11633. SUD-M. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view ]
SUPFAMi SSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEi PS51653. CV_MBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 1 hit.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Suppression of host gene expression by nsp1 proteins of group 2 bat coronaviruses."
    Tohya Y., Narayanan K., Kamitani W., Huang C., Lokugamage K., Makino S.
    J. Virol. 83:5282-5288(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF NSP1.

Entry informationi

Entry nameiR1AB_BC133
AccessioniPrimary (citable) accession number: P0C6W1
Secondary accession number(s): Q0Q4F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: October 29, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3