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P0C6W2

- R1AB_BCHK3

UniProt

P0C6W2 - R1AB_BCHK3

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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Bat coronavirus HKU3 (BtCoV) (SARS-like coronavirus HKU3)
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 similarity
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

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
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.
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
Sitei179 – 1802Cleavage; by PL-PROBy similarity
Sitei818 – 8192Cleavage; by PL-PROBy similarity
Active sitei1645 – 16451For PL-PRO activityPROSITE-ProRule annotation
Active sitei1806 – 18061For PL-PRO activityPROSITE-ProRule annotation
Sitei3234 – 32352Cleavage; by 3CL-PROBy similarity
Active sitei3275 – 32751For 3CL-PRO activityPROSITE-ProRule annotation
Active sitei3379 – 33791For 3CL-PRO activityPROSITE-ProRule annotation
Sitei3540 – 35412Cleavage; by 3CL-PROBy similarity
Sitei3830 – 38312Cleavage; by 3CL-PROBy similarity
Sitei3913 – 39142Cleavage; by 3CL-PROBy similarity
Sitei4111 – 41122Cleavage; by 3CL-PROBy similarity
Sitei4224 – 42252Cleavage; by 3CL-PROBy similarity
Sitei4363 – 43642Cleavage; by 3CL-PROBy similarity
Sitei5295 – 52962Cleavage; by 3CL-PROBy similarity
Sitei5896 – 58972Cleavage; by 3CL-PROBy similarity
Sitei6423 – 64242Cleavage; by 3CL-PROBy similarity
Sitei6769 – 67702Cleavage; by 3CL-PROBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1723 – 176038C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4298 – 431417By similarityAdd
BLAST
Zinc fingeri4341 – 435414By similarityAdd
BLAST
Nucleotide bindingi5577 – 55848ATPBy similarity

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

Protein family/group databases

MEROPSiC16.009.

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 HKU3 (BtCoV) (SARS-like coronavirus HKU3)
Taxonomic identifieri442736 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiRhinolophus sinicus (Chinese rufous horseshoe bat) [TaxID: 89399]
ProteomesiUP000007450: 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 – 179179Host translation inhibitor nsp1By similarityPRO_0000291335Add
BLAST
Chaini180 – 818639Non-structural protein 2By similarityPRO_0000291336Add
BLAST
Chaini819 – 27341916Papain-like proteinaseBy similarityPRO_0000291337Add
BLAST
Chaini2735 – 3234500Non-structural protein 4By similarityPRO_0000291338Add
BLAST
Chaini3235 – 35403063C-like proteinaseBy similarityPRO_0000291339Add
BLAST
Chaini3541 – 3830290Non-structural protein 6By similarityPRO_0000291340Add
BLAST
Chaini3831 – 391383Non-structural protein 7By similarityPRO_0000291341Add
BLAST
Chaini3914 – 4111198Non-structural protein 8By similarityPRO_0000291342Add
BLAST
Chaini4112 – 4224113Non-structural protein 9By similarityPRO_0000291343Add
BLAST
Chaini4225 – 4363139Non-structural protein 10By similarityPRO_0000291344Add
BLAST
Chaini4364 – 5295932RNA-directed RNA polymeraseBy similarityPRO_0000291345Add
BLAST
Chaini5296 – 5896601HelicaseBy similarityPRO_0000291346Add
BLAST
Chaini5897 – 6423527Guanine-N7 methyltransferaseBy similarityPRO_0000291347Add
BLAST
Chaini6424 – 6769346Uridylate-specific endoribonucleaseBy similarityPRO_0000291348Add
BLAST
Chaini6770 – 70672982'-O-methyltransferaseBy similarityPRO_0000291349Add
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

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

ProteinModelPortaliP0C6W2.
SMRiP0C6W2. Positions 13-127, 819-930, 997-1171, 1325-1463, 1535-1846, 3235-3540, 3830-3913, 3915-4105, 4112-4224, 4234-4356, 6424-6767.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2197 – 221721HelicalSequence AnalysisAdd
BLAST
Transmembranei2298 – 231821HelicalSequence AnalysisAdd
BLAST
Transmembranei2345 – 236521HelicalSequence AnalysisAdd
BLAST
Transmembranei2744 – 276421HelicalSequence AnalysisAdd
BLAST
Transmembranei2986 – 300621HelicalSequence AnalysisAdd
BLAST
Transmembranei3016 – 303621HelicalSequence AnalysisAdd
BLAST
Transmembranei3048 – 306821HelicalSequence AnalysisAdd
BLAST
Transmembranei3071 – 309121HelicalSequence AnalysisAdd
BLAST
Transmembranei3099 – 311921HelicalSequence AnalysisAdd
BLAST
Transmembranei3136 – 315621HelicalSequence AnalysisAdd
BLAST
Transmembranei3558 – 357821HelicalSequence AnalysisAdd
BLAST
Transmembranei3580 – 360021HelicalSequence AnalysisAdd
BLAST
Transmembranei3606 – 362621HelicalSequence AnalysisAdd
BLAST
Transmembranei3652 – 367221HelicalSequence AnalysisAdd
BLAST
Transmembranei3679 – 369820HelicalSequence AnalysisAdd
BLAST
Transmembranei3722 – 374221HelicalSequence AnalysisAdd
BLAST
Transmembranei3750 – 377021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini998 – 1164167MacroPROSITE-ProRule annotationAdd
BLAST
Domaini1605 – 1869265Peptidase C16PROSITE-ProRule annotationAdd
BLAST
Domaini3235 – 3540306Peptidase C30PROSITE-ProRule annotationAdd
BLAST
Domaini4975 – 5137163RdRp catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini5296 – 537984CV MBDAdd
BLAST
Domaini5552 – 5733182(+)RNA virus helicase ATP-bindingAdd
BLAST
Domaini5734 – 5903170(+)RNA virus helicase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2086 – 2365280HD1By similarityAdd
BLAST
Regioni2749 – 3156408HD2By similarityAdd
BLAST
Regioni3558 – 3770213HD3By similarityAdd
BLAST
Regioni4906 – 5208303RNA-directed RNA polymeraseBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi930 – 99667Glu-richAdd
BLAST
Compositional biasi2204 – 22074Poly-Leu
Compositional biasi3760 – 37634Poly-Cys

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 fingeri1723 – 176038C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4298 – 431417By similarityAdd
BLAST
Zinc fingeri4341 – 435414By similarityAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR021590. NSP1.
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.
IPR024358. SARS-CoV_Nsp3_N.
IPR022733. SARS_polyprot_cleavage.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF06478. Corona_RPol_N. 1 hit.
PF12379. DUF3655. 1 hit.
PF01661. Macro. 1 hit.
PF11501. Nsp1. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 1 hit.
PF12124. Nsp3_PL2pro. 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.
PF01443. Viral_helicase1. 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: P0C6W2-1) [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
MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT
60 70 80 90 100
CGLVELEKGV LPQLEQPYVF IKRSDALSTN HGHKVVELVA ELDGIQFGRS
110 120 130 140 150
GITLGVLVPH VGETPIAYRN VLLRKNGNKG AGGHSFGIDL KSYDLGDELG
160 170 180 190 200
TDPIEDYEQN WNTKHGSGAL RELTRELNGG VVTRYVDNNF CGPDGYPLEC
210 220 230 240 250
IKDFLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW FTERSEKSYE
260 270 280 290 300
HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
310 320 330 340 350
RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV
360 370 380 390 400
CEGPTTCGYL PTNAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG
410 420 430 440 450
GRTKCFGGCV FSYVGCYNKR AYWVPRASAN IGANHTGITG ENVETLNEDL
460 470 480 490 500
LEILNRERVN INIVGDFRFN EEVAIILASF SASPSAFIET VKGLDYKSFK
510 520 530 540 550
VIVESCGNYK VTNGKPVTGA WNIGQQRSIL TPLCGFPSQA AGVIRSIFSR
560 570 580 590 600
TLDAANHSIL DLQRAAVTTL DGISEQSLRL VDAMVYTSDL LTNSVVVMAY
610 620 630 640 650
VTGGLVQQTM QWLSNMLGTA VDKLKPVFTW VEAKLSAGVE FLRDAWEILK
660 670 680 690 700
FLITGVFDVI KGQIQVATDN IKECVKIFLG VVNKALEMCL DQVTIAGTKL
710 720 730 740 750
RALNLGEVFI AQSRGLYRQC IRGKEQLQLL MPLKAPKEVT FLEGDAHDTV
760 770 780 790 800
LTSEEVVLKS GELEALETPI DSFTSGAVVG TPVCINGLML LELENKEQYC
810 820 830 840 850
ALSPGLLATN NVFRLKGGAP VKGVTFGEDT VLEVQGYKNV KITFELDVRV
860 870 880 890 900
DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTPMGIDLDE
910 920 930 940 950
WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEECEDE EETCEHEYGT
960 970 980 990 1000
EDDYKGLPLE FGASTETPHV EEEEEEEDWL DDAIEAEPEP EPLPEEPVNQ
1010 1020 1030 1040 1050
FVGYLKLTDN VAIKCIDIVK EAQSAKPTVI VNAANTHLKH GGGVAGALNK
1060 1070 1080 1090 1100
ATNGAMQNES DEYIRQNGPL TVGGSCLLSG HNLAEKCLHV VGPNLNAGED
1110 1120 1130 1140 1150
VQLLKRAYEN FNSQDVLLAP LLSAGIFGAK PLQSLKMCVE IVRTQVYLAV
1160 1170 1180 1190 1200
NDKSLYDQIV LDYLDSLKPK VESPNKEEEP KLEEPKAVQP VAEKPVDVKP
1210 1220 1230 1240 1250
KIKACIDEVT TTLEETKFLT NKLLLFADIN GKLYQDSQNM LRGEDMSFLE
1260 1270 1280 1290 1300
KDAPYIVGDV ITSGDITCVI IPAKKSGGTT EMLARALKEV PVAEYITTYP
1310 1320 1330 1340 1350
GQGCAGYTLE EAKTALKKCK SAFYVLPSET PNEKEEVLGT VSWNLREMLA
1360 1370 1380 1390 1400
HAEETRKLMP ICLDVRAIMA TIQRKYKGIK VQEGIVDYGV RFFFYTSKEP
1410 1420 1430 1440 1450
VASIITKLNS LNEPLVTMPI GYVTHGLNLE EAARCMRSLK APAVVSVSSP
1460 1470 1480 1490 1500
DAVTAYNGYL TSSSKTPEEY FVETTSLAGS YRDWSYSGQR TELGVEFLKR
1510 1520 1530 1540 1550
GDKIVYHTTG SPIEFHLDGE VLPLDKLKSL LSLREVKTIK VFTTVDNTNL
1560 1570 1580 1590 1600
HTHIVDMSMT YGQQFGPTYL DGADVTKIKP HVNHEGKTFF VLPSDDTLRS
1610 1620 1630 1640 1650
EAFEYYHTID ESFLGRYMSA LNHTKKWKFP QVGGLTSIKW ADNNCYLSSV
1660 1670 1680 1690 1700
LLALQQVEVK FNAPALQEAY YRARAGDAAN FCALILAYSN KTVGELGDVR
1710 1720 1730 1740 1750
ETMTHLLQHA NLESAKRVLN VVCKHCGQKT TTLKGVEAVM YMGTLSYDEL
1760 1770 1780 1790 1800
KTGVSIPCVC GRNATQYLVQ QESSFVMMSA PPAEYKLQQG AFLCANEYTG
1810 1820 1830 1840 1850
NYQCGHYTHI TAKETLYRVD GAHLTKMSEY KGPVTDVFYK ETSYTTAIKP
1860 1870 1880 1890 1900
VSYKLDGVTY TEIEPKLDGY YKKGNAYYTE QPIDLVPTQP MPNASFDNFK
1910 1920 1930 1940 1950
LTCSNTKFAD DLNQMTGFKK PASRELTVTF FPDLNGDVVA IDYRHYSTSF
1960 1970 1980 1990 2000
KKGAKLVHKP ILWHINQTTN KTTYKPNIWC LRCLWSTKPV DTSNSFEVLV
2010 2020 2030 2040 2050
VEDTQGMDNL ACESQTTTSE EVVENPTVQK EIIECDVKTT EVVGNVILKP
2060 2070 2080 2090 2100
SEEGVKVTQE LGHEDLMAAY VEETSITIKK PNELSLALGL KTLATHGAAA
2110 2120 2130 2140 2150
INSVPWSKIL AYVKPFLGQT AVITSNCIKK CVQRVFSNYM PYVITLLFQL
2160 2170 2180 2190 2200
CTFTKSTNSR IKASLPTTIA KNSVKSVAKL CLDVCINYVK SPKFSKLFTI
2210 2220 2230 2240 2250
VMWLLLLSIC LGSLTYVTAV LGVCLSSLGV PSYCDGVREL YINSSNVTTM
2260 2270 2280 2290 2300
DFCQGYFPCS VCLSGLDSLD SYPALETIQV TISSYKLDLT FLGLAAEWLL
2310 2320 2330 2340 2350
AYMLFTKFFY LLGLSAIMQA FFGYFASHFI SNSWLMWFII SIVQMAPVSA
2360 2370 2380 2390 2400
MVRMYIFFAS FYYVWKSYVH IMDGCTSSTC MMCYKRNRAT RVECTTIVNG
2410 2420 2430 2440 2450
VKRSFYVYAN GGRGFCKAHN WNCLNCDTFC AGSTFISDEV ARDLSLQFKR
2460 2470 2480 2490 2500
PINPTDQSAY VVDSVTVKNG ALHLYFDKAG QKTYERHPLS HFVNLDNLRA
2510 2520 2530 2540 2550
NNTKGSLPIN VIVFDGKSKC EESAAKSASV YYSQLMCQPI LLLDQALVSD
2560 2570 2580 2590 2600
VGDSTEVSVK MFDAYVDTFS ATFSVPMEKL KALVATAHSE LAKGVALDGV
2610 2620 2630 2640 2650
LSTFVSAARQ GVVDTDVDTK DVIECLKLSH HSDIEVTGDS CNNFMLTYNK
2660 2670 2680 2690 2700
VENMTPRDLG ACIDCNARHI NAQVAKSHNV SLVWNVKDYM SLSEQLRKQI
2710 2720 2730 2740 2750
RSAAKKNNIP FRLTCATTRQ VVNVITTKIS LKGGKVVSTW FKLLLKVTLL
2760 2770 2780 2790 2800
CVLAALFCYV IMPVHSLSVH DGYTNEIIGY KAIQDGVTRD IVSTDDCFAN
2810 2820 2830 2840 2850
KHAGFDSWFS QRGGSYRNDK NCPVVAAIIT REIGFIVPGL PGTVLRALNG
2860 2870 2880 2890 2900
DFLHFLPRVF SAVGNICYTP SKLIEYSDFA TSACVLAAEC TIFKDAMGKP
2910 2920 2930 2940 2950
VPYCYDTNLL EGSISYSELR PDTRYVLMDG SIIQFPNTYL EGSVRVVTTF
2960 2970 2980 2990 3000
DAEYCRHGTC ERSEVGVCLS TSGRWVLNNE HYRALPGVFC GVDAMNLIAN
3010 3020 3030 3040 3050
IFTPLVQPVG ALDVSASVVA GGIIAILVTC AAYYFMKFRR AFGEYNHVVA
3060 3070 3080 3090 3100
ANALLFLMSF TILCLAPAYS FLPGVYSIFY LYLTFYFTND VSFLAHLQWF
3110 3120 3130 3140 3150
AMFSPIVPFW ITAIYVFCIS LKHFHWFFSN YLKKRVMFNG VTFSTFEEAA
3160 3170 3180 3190 3200
LCTFLLNKEM YLRLRSETLL PLTQYNRYLA LYNKYKYFSG ALDTTSYREA
3210 3220 3230 3240 3250
ACCHLAKALN DFSNSGADVL YQPPQTSITS AVLQSGFRKM AFPSGKVEGC
3260 3270 3280 3290 3300
MVQVTCGTTT LNGLWLDDTV YCPRHVVCTA EDMLNPNYDD LLIRKSNHSF
3310 3320 3330 3340 3350
LVQAGNVQLR VIGHSMQNCL LRLKVDTSNP KTPKYKFVRI QPGQTFSVLA
3360 3370 3380 3390 3400
CYNGSPSGVY QCAMRPNHTI KGSFLNGSCG SVGFNIDYDC VSFCYMHHME
3410 3420 3430 3440 3450
LPTGVHAGTD LEGKFYGPFV DRQTAQAAGT DTTITLNVLA WLYAAVINGD
3460 3470 3480 3490 3500
RWFLNRFTTT LNDFNLVAMK YNYEPLTQDH VDILGPLSAQ TGIAVLDMCA
3510 3520 3530 3540 3550
ALKELLQNGM NGRTILGSTI LEDEFTPFDV VRQCSGVTFQ GKFKKIVKGT
3560 3570 3580 3590 3600
HHWMLLTFLT SLLILVQSTQ WSLFFFVYEN AFLPFALGIM AVAACAMLLV
3610 3620 3630 3640 3650
KHKHAFLCLF LLPSLATVAY FNMVYMPASW VMRIMTWLEL ADTSLSGYRL
3660 3670 3680 3690 3700
KDCVMYASAL VLLILMTART VYDDAARRVW TLMNVITLVY KVYYGNSLDQ
3710 3720 3730 3740 3750
AISMWALVIS VTSNYSGVVT TIMFLARAIV FVCVEYYPLL FITGNTLQCI
3760 3770 3780 3790 3800
MLVYCFLGYC CCCYFGLFCL LNRYFRLTLG VYDYLVSTQE FRYMNSQGLL
3810 3820 3830 3840 3850
PPKSSIDAFK LNIKLLGIGG KPCIKVATVQ SKMSDVKCTS VVLLSVLQQL
3860 3870 3880 3890 3900
RVESSSKLWA QCVQLHNDIL LAKDTTEAFE KMVSLLSVLL SMQGAVDINK
3910 3920 3930 3940 3950
LCEEMLDNRA TLQAIASEFS SLPSYAAYAT AQEAYEQAVS NGDSEVVLKK
3960 3970 3980 3990 4000
LKKSLNVAKS EFDHDAAMQR KLEKMADQAM TQMYKQARSE DKRAKVTSAM
4010 4020 4030 4040 4050
QTMLFTMLRK LDNDALNNII NNARDGCVPL NIIPLTTAAK LMVVVPDYGT
4060 4070 4080 4090 4100
YKNTCDGNTF TYASALWEIQ QVVDADSKIV QLSEINMDNS PNLAWPLIVT
4110 4120 4130 4140 4150
ALRANSAVKL QNNELSPVAL RQMSCAAGTT QTACTDDNAL AYYNNAKGGR
4160 4170 4180 4190 4200
FVLALLSDHQ DLKWARFPKS DGTGTIYTEL EPPCRFVTDT PKGPKVKYLY
4210 4220 4230 4240 4250
FIKGLNNLNR GMVLGSLAAT VRLQAGNATE VPANSTVLSF CAFAVDPAKA
4260 4270 4280 4290 4300
YKDYLASGGQ PITNCVKMLC THTGTGQAIT VTPEANMDQE SFGGASCCLY
4310 4320 4330 4340 4350
CRCHIDHPNP KGFCDLKGKY VQIPTTCAND PVGFTLRNTV CTVCGMWKGY
4360 4370 4380 4390 4400
GCSCDQLREP MMQSADASTF LNRVCGVSAA RLTPCGTGTS TDVVYRAFDI
4410 4420 4430 4440 4450
YNEKVAGFAK FLKTNCCRFQ EKDEEGNLLD SYFVVKRHTM SNYQHEETIY
4460 4470 4480 4490 4500
NLIKECPAVA VHDFFKFRVD GDMVPHISRQ RLTKYTMADL VYALRHFDEG
4510 4520 4530 4540 4550
NCDTLKEILV TYNCCDDNYF NKKDWYDFVE NPDVLRVYAN LGERVRRALL
4560 4570 4580 4590 4600
KTVQFCDAMR DAGIVGVLTL DNQDLNGNWY DFGDFVQVAP GCGVPIVDSY
4610 4620 4630 4640 4650
YSLLMPILTL TKALAAESHM DADLAKPLVK WDLLKYDFTE ERLCLFDRYF
4660 4670 4680 4690 4700
KYWDQTYHPN CINCLDDRCI LHCANFNVLF STVFPPTSFG PLVRKIFVDG
4710 4720 4730 4740 4750
VPFVVSTGYH FRELGVVHNQ DVNLHSSRLS FKELLVYAAD PAMHAASGNL
4760 4770 4780 4790 4800
LLDKRTTCFS VAALTNNVAF QTVKPGNFNK DFYDFAVSKG FFKEGSSVEL
4810 4820 4830 4840 4850
KHFFFAQDGN AAISDYDYYR YNLPTMCDIR QLLFVVEVVD KYFDCYDGGC
4860 4870 4880 4890 4900
INANQVIVNN LDKSAGFPFN KWGKARLYYD SMSYEDQDAL FAYTKRNVIP
4910 4920 4930 4940 4950
TITQMNLKYA ISAKNRARTV AGVSICSTMT NRQFHQKLLK SIAATRGATV
4960 4970 4980 4990 5000
VIGTSKFYGG WHNMLKTVYS DVESPHLMGW DYPKCDRAMP NMLRIMASLI
5010 5020 5030 5040 5050
LARKHSTCCN LSHRFYRLAN ECAQVLSEMV MCGGSLYVKP GGTSSGDATT
5060 5070 5080 5090 5100
AYANSVFNIC QAVTANVNAL LSTDGNKIAD KYVRNLQHRL YECLYRNRDV
5110 5120 5130 5140 5150
DHEFVDEFYA YLRKHFSMMI LSDDAVVCYN SNYAAQGLVA SIKNFKAVLY
5160 5170 5180 5190 5200
YQNNVFMSEA KCWTETDLTR GPHEFCSQHT MLVKQGDDYV YLPYPDPSRI
5210 5220 5230 5240 5250
LGAGCFVDDI VKTDGTLMIE RFVSLAIDAY PLTKHPNQEY ADVFHLYLQY
5260 5270 5280 5290 5300
IRKLHDELTG HMLDMYSVML TNDNTSRYWE PEFYEAMYTP HTVLQAVGAC
5310 5320 5330 5340 5350
VLCNSQTSLR CGACIRRPFL CCKCCYDHVI STSHKLVLSV NPYVCNAPGC
5360 5370 5380 5390 5400
DVTDVTQLYL GGMSYYCKSH KPPISFPLCA NGQVFGLYKN TCVGSDNVTD
5410 5420 5430 5440 5450
FNAIATCDWT NAGDYILANT CTERLKLFAA ETLKATEETF KLSYGIATVR
5460 5470 5480 5490 5500
EVLSDRELYL SWEVGKPRPP LNRNYVFTGY RVTKNSKVQI GEYTFEKGDY
5510 5520 5530 5540 5550
GDAVVYRGTT TYKLNVGDYF VLTSHTVMPL SAPTLVPQEH YVRITGLYPT
5560 5570 5580 5590 5600
LNISNEFSSN VANYQKIGMQ KYSTLQGPPG TGKSHFAIGL ALYYPSARIV
5610 5620 5630 5640 5650
YTACSHAAVD ALCEKALKYL PIDKCSRIIP ARARVECFDK FKVNSTLEQY
5660 5670 5680 5690 5700
VFCTVNALPE TTADIVVFDE ISMATNYDLS VVNARLRAKH YVYIGDPAQL
5710 5720 5730 5740 5750
PAPRTLLTKG TLEPEYFNSV CRLMKTIGPD MFLGTCRRCP AEIVDTVSAL
5760 5770 5780 5790 5800
VYDNKLKAHK EKSAQCFKMY YKGVITHDVS SAINRPQIGV VREFLTRNPA
5810 5820 5830 5840 5850
WRKAVFISPY NSQNAVASKI LGLPTQTVDS SQGSEYDYVI FTQTTETAHS
5860 5870 5880 5890 5900
CNVNRFNVAI TRAKIGILCI MSDRDLYDKL QFTSLEVPRR NVATLQAENV
5910 5920 5930 5940 5950
TGLFKDCSKI ITGLHPTQAP THLSVDTKFK TEGLCVDIPG IPKDMTYRRL
5960 5970 5980 5990 6000
ISMMGFKMNY QVNGYPNMFI TREEAIRHVR AWIGFDVEGC HATRDAVGTN
6010 6020 6030 6040 6050
LPLQLGFSTG VNLVAVPTGY VDTENSTEFT RVNAKPPPGD QFKHLIPLMY
6060 6070 6080 6090 6100
KGLPWNVVRI KIVQMLSDTL KGLSDRVVFV LWAHGFELTS MKYFVKIGPE
6110 6120 6130 6140 6150
RTCCLCDKRA TCFSTSSDTY ACWNHSVGFD YVYNPFMIDV QQWGFTGNLQ
6160 6170 6180 6190 6200
SNHDQHCQVH GNAHVASCDA IMTRCLAVHE CFVKRVDWSV EYPIIGDELK
6210 6220 6230 6240 6250
INAACRKVQH MVVKSALLAD KFTVLHDIGN PKAIRCVPQA EVDWKFYDAQ
6260 6270 6280 6290 6300
PCSDKAYKIE ELFYSYATHH DKFTDGVCLF WNCNVDRYPA NAIVCRFDTR
6310 6320 6330 6340 6350
VLSNLNLPGC DGGSLYVNKH AFHTPAFDKS AFTHLKQLPF FYYSDSPCES
6360 6370 6380 6390 6400
HGKQVVSDID YVPLKSATCI TRCNLGGAVC RHHANEYRQY LDAYNMMISA
6410 6420 6430 6440 6450
GFSLWIYKQF DTYNLWNTFT KLQSLENVAY NVVNKGHFDG QSGEAPVSII
6460 6470 6480 6490 6500
NNAVYTKVDG IDVEIFENKT TLPVNVAFEL WAKRNIKPVP EIKILNNLGV
6510 6520 6530 6540 6550
DIAANNVIWD YKREAPAHVS TIGVCTMTDI AKKPTESACS SLIVLFDGRV
6560 6570 6580 6590 6600
EGQVDFFRNA RNGVLITEGS VKGLTPSKGP AQASVNGVTL IGESVKTQFN
6610 6620 6630 6640 6650
YFKKVDGIIQ QLPETYFTQS RDLEDFKPRS QMETDFLELA MDEFIQRYKL
6660 6670 6680 6690 6700
EGYAFEHIVY GDFSHGQLGG LHLMIGLAKR SQDSLLKLED FIPMDSTVKN
6710 6720 6730 6740 6750
YFITDAQTGS SKCVCSVIDL LLDDFVEIIK SQDLSVVSKV VKVTIDYAEI
6760 6770 6780 6790 6800
SFMLWCKDGH VETFYPKLQA SQAWQPGVAM PNLYKMQRML LEKCDLQNYG
6810 6820 6830 6840 6850
ENAVIPKGIM MNVAKYTQLC QYLNTLTLAV PYNMRVIHFG AGSDKGVAPG
6860 6870 6880 6890 6900
TAVLRQWLPT GTLLVDSDLN DFVSDADSTL IGDCATVHTA NKWDLIISDM
6910 6920 6930 6940 6950
YDPKTKHVLK DNDSKEGFFT YLCGFIKQKL ALGGSVAVKI TEHSWNADLY
6960 6970 6980 6990 7000
KLMGHFSWWT AFVTNVNASS SEAFLIGVNY LGKPKEQIDG YTMHANYIFW
7010 7020 7030 7040 7050
RNTNPIQLSS YSLFDMSKFP LKLRGTAVMS LKENQINDMI YSLLEKGRLI
7060
IRENNRVVVS SDILVNN

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

Length:7,067
Mass (Da):789,496
Last modified:June 10, 2008 - v1
Checksum:i9EE66BBA1B5E6339
GO
Isoform Replicase polyprotein 1a (identifier: P0C6F8-1) [UniParc]FASTAAdd to Basket

Also known as: pp1a, ORF1a polyprotein

The sequence of this isoform can be found in the external entry P0C6F8.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Length:4,376
Mass (Da):485,585
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ022305 Genomic RNA. Translation: AAY88865.2.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ022305 Genomic RNA. Translation: AAY88865.2 .

3D structure databases

ProteinModelPortali P0C6W2.
SMRi P0C6W2. Positions 13-127, 819-930, 997-1171, 1325-1463, 1535-1846, 3235-3540, 3830-3913, 3915-4105, 4112-4224, 4234-4356, 6424-6767.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C16.009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR021590. NSP1.
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.
IPR024358. SARS-CoV_Nsp3_N.
IPR022733. SARS_polyprot_cleavage.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view ]
Pfami PF06478. Corona_RPol_N. 1 hit.
PF12379. DUF3655. 1 hit.
PF01661. Macro. 1 hit.
PF11501. Nsp1. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 1 hit.
PF12124. Nsp3_PL2pro. 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.
PF01443. Viral_helicase1. 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].
    Strain: Isolate HKU3-1.

Entry informationi

Entry nameiR1AB_BCHK3
AccessioniPrimary (citable) accession number: P0C6W2
Secondary accession number(s): Q3LZX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: October 29, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Bat coronavirus HKU3 is highly similar to SARS-CoV (SARS-like).

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