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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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).PROSITE-ProRule annotationBy similarity
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 a 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 a 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)DescriptionActionsGraphical viewLength
Active sitei1121For PL1-PRO activityPROSITE-ProRule annotation1
Active sitei1272For PL1-PRO activityPROSITE-ProRule annotation1
Active sitei1716For PL2-PRO activityPROSITE-ProRule annotation1
Active sitei1873For PL2-PRO activityPROSITE-ProRule annotation1
Active sitei3374For 3CL-PRO activityPROSITE-ProRule annotation1
Active sitei3478For 3CL-PRO activity1
Metal bindingi5387Zinc 1PROSITE-ProRule annotation1
Metal bindingi5390Zinc 1PROSITE-ProRule annotation1
Metal bindingi5398Zinc 2PROSITE-ProRule annotation1
Metal bindingi5401Zinc 1PROSITE-ProRule annotation1
Metal bindingi5408Zinc 1PROSITE-ProRule annotation1
Metal bindingi5411Zinc 2PROSITE-ProRule annotation1
Metal bindingi5415Zinc 2PROSITE-ProRule annotation1
Metal bindingi5421Zinc 2PROSITE-ProRule annotation1
Metal bindingi5432Zinc 3PROSITE-ProRule annotation1
Metal bindingi5437Zinc 3PROSITE-ProRule annotation1
Metal bindingi5454Zinc 3PROSITE-ProRule annotation1
Metal bindingi5457Zinc 3PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1198 – 1226C4-type 1PROSITE-ProRule annotationAdd BLAST29
Zinc fingeri1794 – 1830C4-type 2PROSITE-ProRule annotationAdd BLAST37
Zinc fingeri4391 – 4407By similarityAdd BLAST17
Zinc fingeri4433 – 4446By similarityAdd BLAST14
Nucleotide bindingi5663 – 5670ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Helicase, Hydrolase, Methyltransferase, 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):
p28
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p65
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
p210
Non-structural protein 4
Short name:
nsp4
Alternative name(s):
Peptide HD2
p44
3C-like proteinase (EC:3.4.22.-)
Short name:
3CL-PRO
Short name:
3CLp
Alternative name(s):
M-PRO
nsp5
p27
Non-structural protein 6
Short name:
nsp6
Non-structural protein 7
Short name:
nsp7
Alternative name(s):
p10
Non-structural protein 8
Short name:
nsp8
Alternative name(s):
p22
Non-structural protein 9
Short name:
nsp9
Alternative name(s):
p12
Non-structural protein 10
Short name:
nsp10
Alternative name(s):
Growth factor-like peptide
Short name:
GFL
p15
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
Pol
Short name:
RdRp
Alternative name(s):
nsp12
p100
Helicase (EC:3.6.4.12, EC:3.6.4.13)
Short name:
Hel
Alternative name(s):
nsp13
p67
Alternative name(s):
nsp14
Alternative name(s):
NendoU
nsp15
p35
Alternative name(s):
nsp16
Gene namesi
Name:rep
ORF Names:1a-1b
OrganismiMurine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus)
Taxonomic identifieri11142 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
Proteomesi
  • UP000007192 Componenti: Genome

Subcellular locationi

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.
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.
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.
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.
Helicase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei2225 – 2245HelicalSequence analysisAdd BLAST21
Transmembranei2286 – 2306HelicalSequence analysisAdd BLAST21
Transmembranei2314 – 2334HelicalSequence analysisAdd BLAST21
Transmembranei2400 – 2420HelicalSequence analysisAdd BLAST21
Transmembranei2442 – 2462HelicalSequence analysisAdd BLAST21
Transmembranei2625 – 2645HelicalSequence analysisAdd BLAST21
Transmembranei2847 – 2867HelicalSequence analysisAdd BLAST21
Transmembranei3096 – 3116HelicalSequence analysisAdd BLAST21
Transmembranei3118 – 3138HelicalSequence analysisAdd BLAST21
Transmembranei3150 – 3170HelicalSequence analysisAdd BLAST21
Transmembranei3177 – 3197HelicalSequence analysisAdd BLAST21
Transmembranei3202 – 3222HelicalSequence analysisAdd BLAST21
Transmembranei3644 – 3664HelicalSequence analysisAdd BLAST21
Transmembranei3674 – 3694HelicalSequence analysisAdd BLAST21
Transmembranei3699 – 3719HelicalSequence analysisAdd BLAST21
Transmembranei3742 – 3762HelicalSequence analysisAdd BLAST21
Transmembranei3769 – 3789HelicalSequence analysisAdd BLAST21
Transmembranei3796 – 3816HelicalSequence analysisAdd BLAST21
Transmembranei3840 – 3860HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3331F → A, H or W: No effect. 1 Publication1
Mutagenesisi3332L → I or S: No processing between peptide HD2 and 3CL-PRO. 1 Publication1
Mutagenesisi3333Q → A, K or R: No processing between peptide HD2 and 3CL-PRO. 1 Publication1
Mutagenesisi3334S → A: No effect. 1 Publication1
Mutagenesisi3334S → C: No processing between peptide HD2 and 3CL-PRO. 1 Publication1
Mutagenesisi3335G → A: No effect. 1 Publication1
Mutagenesisi3335G → P: No processing between peptide HD2 and 3CL-PRO. 1 Publication1
Mutagenesisi3336I → L: No effect. 1 Publication1
Mutagenesisi3478C → A: Complete loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi5381L → I: No processing between RDRP and helicase. 1 Publication1
Mutagenesisi5381L → M: No effect. 1 Publication1
Mutagenesisi5382Q → K or R: No processing between RDRP and helicase. 1 Publication1
Mutagenesisi5383S → A: No effect. 1 Publication1
Mutagenesisi5383S → N: No processing between RDRP and helicase. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000373381 – 247Host translation inhibitor nsp1By similarityAdd BLAST247
ChainiPRO_0000037339248 – 832Non-structural protein 2By similarityAdd BLAST585
ChainiPRO_0000037340833 – 2837Papain-like proteinaseBy similarityAdd BLAST2005
ChainiPRO_00000373412838 – 3333Non-structural protein 4By similarityAdd BLAST496
ChainiPRO_00000373423334 – 36353C-like proteinaseBy similarityAdd BLAST302
ChainiPRO_00000373433636 – 3921Non-structural protein 6By similarityAdd BLAST286
ChainiPRO_00000373443922 – 4013Non-structural protein 7By similarityAdd BLAST92
ChainiPRO_00000373454014 – 4207Non-structural protein 8By similarityAdd BLAST194
ChainiPRO_00000373464208 – 4317Non-structural protein 9By similarityAdd BLAST110
ChainiPRO_00000373474318 – 4454Non-structural protein 10By similarityAdd BLAST137
ChainiPRO_00000373484455 – 5382RNA-directed RNA polymeraseBy similarityAdd BLAST928
ChainiPRO_00000373495383 – 5982HelicaseBy similarityAdd BLAST600
ChainiPRO_00000373505983 – 6503Guanine-N7 methyltransferaseBy similarityAdd BLAST521
ChainiPRO_00000373516504 – 6877Uridylate-specific endoribonucleaseBy similarityAdd BLAST374
ChainiPRO_00000373526878 – 71762'-O-methyltransferaseBy similarityAdd BLAST299

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei247 – 248Cleavage; by PL1-PROCurated2
Sitei832 – 833Cleavage; by PL1-PROCurated2
Sitei2837 – 2838Cleavage; by PL2-PRO2
Sitei3333 – 3334Cleavage; by 3CL-PRO2
Sitei3635 – 3636Cleavage; by 3CL-PRO2
Sitei3921 – 3922Cleavage; by 3CL-PRO2
Sitei4013 – 4014Cleavage; by 3CL-PRO2
Sitei4207 – 4208Cleavage; by 3CL-PRO2
Sitei4317 – 4318Cleavage; by 3CL-PRO2
Sitei4454 – 4455Cleavage; by 3CL-PRO2
Sitei5382 – 5383Cleavage; by 3CL-PRO2
Sitei5982 – 5983Cleavage; by 3CL-PROCurated2
Sitei6503 – 6504Cleavage; by 3CL-PROCurated2
Sitei6877 – 6878Cleavage; by 3CL-PROCurated2

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

Secondary structure

17176
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1537 – 1545Combined sources9
Beta strandi1556 – 1563Combined sources8
Beta strandi1566 – 1574Combined sources9
Turni1575 – 1577Combined sources3
Beta strandi1578 – 1583Combined sources6
Beta strandi1586 – 1591Combined sources6
Beta strandi1594 – 1597Combined sources4
Helixi1600 – 1607Combined sources8
Beta strandi1610 – 1621Combined sources12
Beta strandi1623 – 1628Combined sources6
Helixi1633 – 1637Combined sources5
Beta strandi1639 – 1642Combined sources4
Helixi1654 – 1656Combined sources3
Beta strandi1660 – 1663Combined sources4
Helixi1669 – 1678Combined sources10
Helixi1683 – 1695Combined sources13
Beta strandi1700 – 1703Combined sources4
Beta strandi1706 – 1709Combined sources4
Helixi1716 – 1725Combined sources10
Helixi1735 – 1745Combined sources11
Helixi1750 – 1759Combined sources10
Helixi1770 – 1780Combined sources11
Beta strandi1787 – 1794Combined sources8
Beta strandi1797 – 1804Combined sources8
Helixi1806 – 1809Combined sources4
Beta strandi1810 – 1813Combined sources4
Helixi1817 – 1822Combined sources6
Beta strandi1824 – 1828Combined sources5
Beta strandi1831 – 1841Combined sources11
Beta strandi1845 – 1852Combined sources8
Beta strandi1861 – 1867Combined sources7
Turni1869 – 1872Combined sources4
Beta strandi1873 – 1878Combined sources6
Beta strandi1880 – 1882Combined sources3
Beta strandi1884 – 1887Combined sources4
Beta strandi1890 – 1893Combined sources4
Beta strandi1901 – 1906Combined sources6
Helixi3246 – 3249Combined sources4
Beta strandi3254 – 3256Combined sources3
Helixi3258 – 3267Combined sources10
Helixi3270 – 3278Combined sources9
Helixi3280 – 3284Combined sources5
Beta strandi3287 – 3290Combined sources4
Helixi3292 – 3313Combined sources22
Beta strandi3318 – 3320Combined sources3
Beta strandi3326 – 3330Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GTHX-ray2.70A6504-6872[»]
2GTIX-ray2.15A6504-6872[»]
3VC8X-ray2.00A/B3245-3333[»]
3VCBX-ray2.40A/B3245-3333[»]
4YPTX-ray2.60A1525-1911[»]
ProteinModelPortaliP0C6X9.
SMRiP0C6X9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C6X9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1084 – 1333Peptidase C16 1PROSITE-ProRule annotationAdd BLAST250
Domaini1323 – 1482MacroPROSITE-ProRule annotationAdd BLAST160
Domaini1678 – 1937Peptidase C16 2PROSITE-ProRule annotationAdd BLAST260
Domaini3334 – 3635Peptidase C30PROSITE-ProRule annotationAdd BLAST302
Domaini5062 – 5224RdRp catalyticPROSITE-ProRule annotationAdd BLAST163
Domaini5383 – 5466CV ZBDPROSITE-ProRule annotationAdd BLAST84
Domaini5638 – 5819(+)RNA virus helicase ATP-bindingAdd BLAST182
Domaini5820 – 5989(+)RNA virus helicase C-terminalAdd BLAST170

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2225 – 2645HD1Add BLAST421
Regioni2847 – 3222HD2Add BLAST376
Regioni3526 – 3860HD3Add BLAST335

Domaini

The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.

Sequence similaritiesi

Contains 1 CV ZBD (coronavirus zinc-binding) domain.PROSITE-ProRule annotation
Contains 1 Macro domain.PROSITE-ProRule annotation
Contains 2 peptidase C16 domains.PROSITE-ProRule annotation
Contains 1 peptidase C30 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1198 – 1226C4-type 1PROSITE-ProRule annotationAdd BLAST29
Zinc fingeri1794 – 1830C4-type 2PROSITE-ProRule annotationAdd BLAST37
Zinc fingeri4391 – 4407By similarityAdd BLAST17
Zinc fingeri4433 – 4446By similarityAdd BLAST14

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR022570. B-CoV_NSP1.
IPR032505. Corona_NSP4_C.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR032592. NAR_dom.
IPR009466. NSP11.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR002705. Pept_C30/C16_B_coronavir.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR009003. Peptidase_S1_PA.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF16348. Corona_NSP4_C. 1 hit.
PF06478. Corona_RPol_N. 1 hit.
PF11963. DUF3477. 2 hits.
PF01661. Macro. 1 hit.
PF16251. NAR. 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.
PF01831. Peptidase_C16. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF00680. RdRP_1. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMiSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 2 hits.
PROSITEiPS51653. CV_ZBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
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: P0C6X9-1) [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
MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK
60 70 80 90 100
GKTLVNHVRV NCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG
110 120 130 140 150
SAVLVKPSKR LSIQAWTNLG VLPKTAAMGL FKRVCLCNTR ECSCDAHVAF
160 170 180 190 200
HLFTVQPDGV CLGNGRFIGW FVPVTAIPEY AKQWLQPWSI LLRKGGNKGS
210 220 230 240 250
VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSCKAYA LLKGYRGVKP
260 270 280 290 300
ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELFPVWRDS LDSEVLVAWH
310 320 330 340 350
VDRDPRAAMR LQTLATVRCI DYVGQPTEDV VDGDVVVREP AHLLAANAIV
360 370 380 390 400
KRLPRLVETM LYTDSSVTEF CYKTKLCECG FITQFGYVDC CGDTCDFRGW
410 420 430 440 450
VAGNMMDGFP CPGCTKNYMP WELEAQSSGV IPEGGVLFTQ STDTVNRESF
460 470 480 490 500
KLYGHAVVPF GSAVYWSPCP GMWLPVIWSS VKSYSGLTYT GVVGCKAIVQ
510 520 530 540 550
ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN RGDYSLLLEN
560 570 580 590 600
VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN
610 620 630 640 650
FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT
660 670 680 690 700
EWFDLAVDIA ASAAGWLCYQ LVNGLFAVAN GVITFVQEVP ELVKNFVDKF
710 720 730 740 750
KAFFKVLIDS MSVSILSGLT VVKTASNRVC LAGSKVYEVV QKSLSAYVMP
760 770 780 790 800
VGCSEATCLV GEIEPAVFED DVVDVVKAPL TYQGCCKPPT SFEKICIVDK
810 820 830 840 850
LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVEFND KPKVRKIPST
860 870 880 890 900
RKIKITFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC
910 920 930 940 950
KEHDVIGTKV CALLDRLAGD YVYLFDEGGD EVIAPRMYCS FSAPDDEDCV
960 970 980 990 1000
AADVVDADEN QDDDAEDSAV LVADTQEEDG VAKGQVEADS EICVAHTGSQ
1010 1020 1030 1040 1050
EELAEPDAVG SQTPIASAEE TEVGEASDRE GIAEAKATVC ADAVDACPDQ
1060 1070 1080 1090 1100
VEAFEIEKVE DSILDELQTE LNAPADKTYE DVLAFDAVCS EALSAFYAVP
1110 1120 1130 1140 1150
SDETHFKVCG FYSPAIERTN CWLRSTLIVM QSLPLEFKDL EMQKLWLSYK
1160 1170 1180 1190 1200
AGYDQCFVDK LVKSVPKSII LPQGGYVADF AYFFLSQCSF KAYANWRCLE
1210 1220 1230 1240 1250
CDMELKLQGL DAMFFYGDVV SHMCKCGNSM TLLSADIPYT LHFGVRDDKF
1260 1270 1280 1290 1300
CAFYTPRKVF RAACAVDVND CHSMAVVEGK QIDGKVVTKF IGDKFDFMVG
1310 1320 1330 1340 1350
YGMTFSMSPF ELAQLYGSCI TPNVCFVKGD VIKVVRLVNA EVIVNPANGR
1360 1370 1380 1390 1400
MAHGAGVAGA IAEKAGSAFI KETSDMVKAQ GVCQVGECYE SAGGKLCKKV
1410 1420 1430 1440 1450
LNIVGPDARG HGKQCYSLLE RAYQHINKCD NVVTTLISAG IFSVPTDVSL
1460 1470 1480 1490 1500
TYLLGVVTKN VILVSNNQDD FDVIEKCQVT SVAGTKALSL QLAKNLCRDV
1510 1520 1530 1540 1550
KFVTNACSSL FSESCFVSSY DVLQEVEALR HDIQLDDDAR VFVQANMDCL
1560 1570 1580 1590 1600
PTDWRLVNKF DSVDGVRTIK YFECPGGIFV SSQGKKFGYV QNGSFKEASV
1610 1620 1630 1640 1650
SQIRALLANK VDVLCTVDGV NFRSCCVAEG EVFGKTLGSV FCDGINVTKV
1660 1670 1680 1690 1700
RCSAIYKGKV FFQYSDLSEA DLVAVKDAFG FDEPQLLKYY TMLGMCKWPV
1710 1720 1730 1740 1750
VVCGNYFAFK QSNNNCYINV ACLMLQHLSL KFPKWQWQEA WNEFRSGKPL
1760 1770 1780 1790 1800
RFVSLVLAKG SFKFNEPSDS IDFMRVVLRE ADLSGATCNL EFVCKCGVKQ
1810 1820 1830 1840 1850
EQRKGVDAVM HFGTLDKGDL VRGYNIACTC GSKLVHCTQF NVPFLICSNT
1860 1870 1880 1890 1900
PEGRKLPDDV VAANIFTGGS VGHYTHVKCK PKYQLYDACN VNKVSEAKGN
1910 1920 1930 1940 1950
FTDCLYLKNL KQTFSSVLTT FYLDDVKCVE YKPDLSQYYC ESGKYYTKPI
1960 1970 1980 1990 2000
IKAQFRTFEK VDGVYTNFKL VGHSIAEKLN AKLGFDCNSP FVEYKITEWP
2010 2020 2030 2040 2050
TATGDVVLAS DDLYVSRYSS GCITFGKPVV WLGHEEASLK SLTYFNRPSV
2060 2070 2080 2090 2100
VCENKFNVLP VDVSEPTDKG PVPAAVLVTG VPGADASAGA GIAKEQKACA
2110 2120 2130 2140 2150
SASVEDQVVT EVRQEPSVSA ADVKEVKLNG VKKPVKVEGS VVVNDPTSET
2160 2170 2180 2190 2200
KVVKSLSIVD VYDMFLTGCK YVVWTANELS RLVNSPTVRE YVKWGMGKIV
2210 2220 2230 2240 2250
TPAKLLLLRD EKQEFVAPKV VKAKAIACYC AVKWFLLYCF SWIKFNTDNK
2260 2270 2280 2290 2300
VIYTTEVASK LTFKLCCLAF KNALQTFNWS VVSRGFFLVA TVFLLWFNFL
2310 2320 2330 2340 2350
YANVILSDFY LPNIGPLPTF VGQIVAWFKT TFGVSTICDF YQVTDLGYRS
2360 2370 2380 2390 2400
SFCNGSMVCE LCFSGFDMLD NYDAINVVQH VVDRRLSFDY ISLFKLVVEL
2410 2420 2430 2440 2450
VIGYSLYTVC FYPLFVLIGM QLLTTWLPEF FMLETMHWSA RLFVFVANML
2460 2470 2480 2490 2500
PAFTLLRFYI VVTAMYKVYC LCRHVMYGCS KPGCLFCYKR NRSVRVKCST
2510 2520 2530 2540 2550
VVGGSLRYYD VMANGGTGFC TKHQWNCLNC NSWKPGNTFI THEAAADLSK
2560 2570 2580 2590 2600
ELKRPVNPTD SAYYSVTEVK QVGCSMRLFY ERDGQRVYDD VNASLFVDMN
2610 2620 2630 2640 2650
GLLHSKVKGV PETHVVVVEN EADKAGFLGA AVFYAQSLYR PMLMVEKKLI
2660 2670 2680 2690 2700
TTANTGLSVS RTMFDLYVDS LLNVLDVDRK SLTSFVNAAH NSLKEGVQLE
2710 2720 2730 2740 2750
QVMDTFIGCA RRKCAIDSDV ETKSITKSVM SAVNAGVDFT DESCNNLVPT
2760 2770 2780 2790 2800
YVKSDTIVAA DLGVLIQNNA KHVQANVAKA ANVACIWSVD AFNQLSADLQ
2810 2820 2830 2840 2850
HRLRKACSKT GLKIKLTYNK QEANVPILTT PFSLKGGAVF SRMLQWLFVA
2860 2870 2880 2890 2900
NLICFIVLWA LMPTYAVHKS DMQLPLYASF KVIDNGVLRD VSVTDACFAN
2910 2920 2930 2940 2950
KFNQFDQWYE STFGLAYYRN SKACPVVVAV IDQDIGHTLF NVPTTVLRYG
2960 2970 2980 2990 3000
FHVLHFITHA FATDSVQCYT PHMQIPYDNF YASGCVLSSL CTMLAHADGT
3010 3020 3030 3040 3050
PHPYCYTGGV MHNASLYSSL APHVRYNLAS SNGYIRFPEV VSEGIVRVVR
3060 3070 3080 3090 3100
TRSMTYCRVG LCEEAEEGIC FNFNRSWVLN NPYYRAMPGT FCGRNAFDLI
3110 3120 3130 3140 3150
HQVLGGLVRP IDFFALTASS VAGAILAIIV VLAFYYLIKL KRAFGDYTSV
3160 3170 3180 3190 3200
VVINVIVWCI NFLMLFVFQV YPTLSCLYAC FYFYTTLYFP SEISVVMHLQ
3210 3220 3230 3240 3250
WLVMYGAIMP LWFCIIYVAV VVSNHALWLF SYCRKIGTEV RSDGTFEEMA
3260 3270 3280 3290 3300
LTTFMITKES YCKLKNSVSD VAFNRYLSLY NKYRYFSGKM DTAAYREAAC
3310 3320 3330 3340 3350
SQLAKAMETF NHNNGNDVLY QPPTASVTTS FLQSGIVKMV SPTSKVEPCI
3360 3370 3380 3390 3400
VSVTYGNMTL NGLWLDDKVY CPRHVICSSA DMTDPDYPNL LCRVTSSDFC
3410 3420 3430 3440 3450
VMSGRMSLTV MSYQMQGCQL VLTVTLQNPN TPKYSFGVVK PGETFTVLAA
3460 3470 3480 3490 3500
YNGRPQGAFH VTLRSSHTIK GSFLCGSCGS VGYVLTGDSV RFVYMHQLEL
3510 3520 3530 3540 3550
STGCHTGTDF SGNFYGPYRD AQVVQLPVQD YTQTVNVVAW LYAAIFNRCN
3560 3570 3580 3590 3600
WFVQSDSCSL EEFNVWAMTN GFSSIKADLV LDALASMTGV TVEQVLAAIK
3610 3620 3630 3640 3650
RLHSGFQGKQ ILGSCVLEDE TPSDVYQQLA GVKLQSKRTR VIKGTCCWIL
3660 3670 3680 3690 3700
ASTFLFCSII SAFVKWTMFM YVTTHMLGVT LCALCFVSFA MLLIKHKHLY
3710 3720 3730 3740 3750
LTMYIMPVLC TFYTNYLVVY KQSFRGLAYA WLSHFVPAVD YTYMDEVLYG
3760 3770 3780 3790 3800
VVLLVAMVFV TMRSINHDVF SIMFLVGRLV SLVSMWYFGA NLEEEVLLFL
3810 3820 3830 3840 3850
TSLFGTYTWT TMLSLATAKV IAKWLAVNVL YFTDVPQIKL VLLSYLCIGY
3860 3870 3880 3890 3900
VCCCYWGILS LLNSIFRMPL GVYNYKISVQ ELRYMNANGL RPPRNSFEAL
3910 3920 3930 3940 3950
MLNFKLLGIG GVPVIEVSQI QSRLTDVKCA NVVLLNCLQH LHIASNSKLW
3960 3970 3980 3990 4000
QYCSTLHNEI LATSDLSMAF DKLAQLLVVL FANPAAVDSK CLASIEEVSD
4010 4020 4030 4040 4050
DYVRDNTVLQ ALQSEFVNMA SFVEYELAKK NLDEAKASGS ANQQQIKQLE
4060 4070 4080 4090 4100
KACNIAKSAY ERDRAVARKL ERMADLALTN MYKEARINDK KSKVVSALQT
4110 4120 4130 4140 4150
MLFSMVRKLD NQALNSILDN AVKGCVPLNA IPSLTSNTLT IIVPDKQVFD
4160 4170 4180 4190 4200
QVVDNVYVTY AGNVWHIQFI QDADGAVKQL NEIDVNSTWP LVIAANRHNE
4210 4220 4230 4240 4250
VSTVVLQNNE LMPQKLRTQV VNSGSDMNCN TPTQCYYNTT GTGKIVYAIL
4260 4270 4280 4290 4300
SDCDGLKYTK IVKEDGNCVV LELDPPCKFS VQDVKGLKIK YLYFVKGCNT
4310 4320 4330 4340 4350
LARGWVVGTL SSTVRLQAGT ATEYASNSAI LSLCAFSVDP KKTYLDYIKQ
4360 4370 4380 4390 4400
GGVPVTNCVK MLCDHAGTGM AITIKPEATT NQDSYGGASV CIYCRSRVEH
4410 4420 4430 4440 4450
PDVDGLCKLR GKFVQVPLGI KDPVSYVLTH DVCQVCGFWR DGSCSCVGTG
4460 4470 4480 4490 4500
SQFQSKDTNF LNRIRGTSVN ARLVPCASGL DTDVQLRAFD ICNANRAGIG
4510 4520 4530 4540 4550
LYYKVNCCRF QRVDEDGNKL DKFFVVKRTN LEVYNKEKEC YELTKECGVV
4560 4570 4580 4590 4600
AEHEFFTFDV EGSRVPHIVR KDLSKFTMLD LCYALRHFDR NDCSTLKEIL
4610 4620 4630 4640 4650
LTYAECEESY FQKKDWYDFV ENPDIINVYK KLGPIFNRAL LNTAKFADAL
4660 4670 4680 4690 4700
VEAGLVGVLT LDNQDLYGQW YDFGDFVKTV PGCGVAVADS YYSYMMPMLT
4710 4720 4730 4740 4750
MCHALDSELF VNGTYREFDL VQYDFTDFKL ELFTKYFKHW SMTYHPNTCE
4760 4770 4780 4790 4800
CEDDRCIIHC ANFNILFSMV LPKTCFGPLV RQIFVDGVPF VVSIGYHYKE
4810 4820 4830 4840 4850
LGVVMNMDVD THRYRLSLKD LLLYAADPAL HVASASALLD LRTCCFSVAA
4860 4870 4880 4890 4900
ITSGVKFQTV KPGNFNQDFY EFILSKGLLK EGSSVDLKHF FFTQDGNAAI
4910 4920 4930 4940 4950
TDYNYYKYNL PTMVDIKQLL FVLEVVNKYF EIYEGGCIPA TQVIVNNYDK
4960 4970 4980 4990 5000
SAGYPFNKFG KARLYYEALS FEEQDEIYAY TKRNVLPTLT QMNLKYAISA
5010 5020 5030 5040 5050
KNRARTVAGV SILSTMTGRM FHQKCLKSIA ATRGVPVVIG TTKFYGGWDD
5060 5070 5080 5090 5100
MLRRLIKDVD SPVLMGWDYP KCDRAMPNIL RIVSSLVLAR KHDSCCSHTD
5110 5120 5130 5140 5150
RFYRLANECA QVLSEIVMCG GCYYVKPGGT SSGDATTAFA NSVFNICQAV
5160 5170 5180 5190 5200
SANVCSLMAC NGHKIEDLSI RELQKRLYSN VYRADHVDPA FVSEYYEFLN
5210 5220 5230 5240 5250
KHFSMMILSD DGVVCYNSEF ASKGYIANIS AFQQVLYYQN NVFMSEAKCW
5260 5270 5280 5290 5300
VETDIEKGPH EFCSQHTMLV KMDGDEVYLP YPDPSRILGA GCFVDDLLKT
5310 5320 5330 5340 5350
DSVLLIERFV SLAIDAYPLV YHENPEYQNV FRVYLEYIKK LYNDLGNQIL
5360 5370 5380 5390 5400
DSYSVILSTC DGQKFTDETF YKNMYLRSAV LQSVGACVVC SSQTSLRCGS
5410 5420 5430 5440 5450
CIRKPLLCCK CAYDHVMSTD HKYVLSVSPY VCNSPGCDVN DVTKLYLGGM
5460 5470 5480 5490 5500
SYYCEDHKPQ YSFKLVMNGM VFGLYKQSCT GSPYIEDFNK IASCKWTEVD
5510 5520 5530 5540 5550
DYVLANECTE RLKLFAAETQ KATEEAFKQC YASATIREIV SDRELILSWE
5560 5570 5580 5590 5600
IGKVRPPLNK NYVFTGYHFT NNGKTVLGEY VFDKSELTNG VYYRATTTYK
5610 5620 5630 5640 5650
LSVGDVFILT SHAVSSLSAP TLVPQENYTS IRFASVYSVP ETFQNNVPNY
5660 5670 5680 5690 5700
QHIGMKRYCT VQGPPGTGKS HLAIGLAVYY CTARVVYTAA SHAAVDALCE
5710 5720 5730 5740 5750
KAHKFLNIND CTRIVPAKVR VDCYDKFKVN DTTRKYVFTT INALPELVTD
5760 5770 5780 5790 5800
IIVVDEVSML TNYELSVINS RVRAKHYVYI GDPAQLPAPR VLLNKGTLEP
5810 5820 5830 5840 5850
RYFNSVTKLM CCLGPDIFLG TCYRCPKEIV DTVSALVYNN KLKAKNDNSS
5860 5870 5880 5890 5900
MCFKVYYKGQ TTHESSSAVN MQQIHLISKF LKANPSWSNA VFISPYNSQN
5910 5920 5930 5940 5950
YVAKRVLGLQ TQTVDSAQGS EYDFVIYSQT AETAHSVNVN RFNVAITRAK
5960 5970 5980 5990 6000
KGILCVMSSM QLFESLNFTT LTLDKINNPR LQCTTNLFKD CSRSYVGYHP
6010 6020 6030 6040 6050
AHAPSFLAVD DKYKVGGDLA VCLNVADSAV TYSRLISLMG FKLDLTLDGY
6060 6070 6080 6090 6100
CKLFITRDEA IKRVRAWVGF DAEGAHAIRD SIGTNFPLQL GFSTGIDFVV
6110 6120 6130 6140 6150
EATGMFAERD GYVFKKAAAR APPGEQFKHL IPLMSRGQKW DVVRIRIVQM
6160 6170 6180 6190 6200
LSDHLVDLAD SVVLVTWAAS FELTCLRYFA KVGREVVCSV CTKRATCFNS
6210 6220 6230 6240 6250
RTGYYGCWRH SYSCDYLYNP LIVDIQQWGY TGSLTSNHDP ICSVHKGAHV
6260 6270 6280 6290 6300
ASSDAIMTRC LAVHDCFCKS VNWNLEYPII SNEVSVNTSC RLLQRVMFRA
6310 6320 6330 6340 6350
AMLCNRYDVC YDIGNPKGLA CVKGYDFKFY DASPVVKSVK QFVYKYEAHK
6360 6370 6380 6390 6400
DQFLDGLCMF WNCNVDKYPA NAVVCRFDTR VLNKLNLPGC NGGSLYVNKH
6410 6420 6430 6440 6450
AFHTSPFTRA AFENLKPMPF FYYSDTPCVY MEGMESKQVD YVPLRSATCI
6460 6470 6480 6490 6500
TRCNLGGAVC LKHAEEYREY LESYNTATTA GFTFWVYKTF DFYNLWNTFT
6510 6520 6530 6540 6550
RLQSLENVVY NLVNAGHFDG RAGELPCAVI GEKVIAKIQN EDVVVFKNNT
6560 6570 6580 6590 6600
PFPTNVAVEL FAKRSIRPHP ELKLFRNLNI DVCWSHVLWD YAKDSVFCSS
6610 6620 6630 6640 6650
TYKVCKYTDL QCIESLNVLF DGRDNGALEA FKKCRNGVYI NTTKIKSLSM
6660 6670 6680 6690 6700
IKGPQRADLN GVVVEKVGDS DVEFWFAVRK DGDDVIFSRT GSLEPSHYRS
6710 6720 6730 6740 6750
PQGNPGGNRV GDLSGNEALA RGTIFTQSRL LSSFTPRSEM EKDFMDLDDD
6760 6770 6780 6790 6800
VFIAKYSLQD YAFEHVVYGS FNQKIIGGLH LLIGLARRQQ KSNLVIQEFV
6810 6820 6830 6840 6850
TYDSSIHSYF ITDENSGSSK SVCTVIDLLL DDFVDIVKSL NLKCVSKVVN
6860 6870 6880 6890 6900
VNVDFKDFQF MLWCNEEKVM TFYPRLQAAA DWKPGYVMPV LYKYLESPLE
6910 6920 6930 6940 6950
RVNLWNYGKP ITLPTGCMMN VAKYTQLCQY LSTTTLAVPA NMRVLHLGAG
6960 6970 6980 6990 7000
SDKGVAPGSA VLRQWLPAGS ILVDNDVNPF VSDSVASYYG NCITLPFDCQ
7010 7020 7030 7040 7050
WDLIISDMYD PLTKNIGEYN VSKDGFFTYL CHLIRDKLAL GGSVAIKITE
7060 7070 7080 7090 7100
FSWNAELYSL MGKFAFWTIF CTNVNASSSE GFLIGINWLN KTRTEIDGKT
7110 7120 7130 7140 7150
MHANYLFWRN STMWNGGAYS LFDMSKFPLK AAGTAVVSLK PDQINDLVLS
7160 7170
LIEKGKLLVR DTRKEVFVGD SLVNVK
Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.
Length:7,176
Mass (Da):802,596
Last modified:June 10, 2008 - v1
Checksum:iAE90461FA631BED3
GO
Isoform Replicase polyprotein 1a (identifier: P0C6V0-1) [UniParc]FASTAAdd to basket
Also known as: pp1a, ORF1a polyprotein
The sequence of this isoform can be found in the external entry P0C6V0.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:4,468
Mass (Da):496,341
GO

Sequence cautioni

The sequence AAB86818 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAB86820 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAA36202 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti287 – 288WR → CA (PubMed:2545027).Curated2
Sequence conflicti311L → V (PubMed:2545027).Curated1
Sequence conflicti570D → G (PubMed:2545027).Curated1
Sequence conflicti3620E → EL (PubMed:9426441).Curated1
Sequence conflicti3711T → TL (PubMed:9426441).Curated1
Sequence conflicti3968M → V (PubMed:9426441).Curated1
Sequence conflicti4464I → V (PubMed:9426441).Curated1
Sequence conflicti6156V → A (PubMed:9426441).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti1699P → S in strain: Isolate C12 mutant. 1
Natural varianti2196M → K in strain: Isolate C12 mutant. 1
Natural varianti5773R → S in strain: Isolate C12 mutant. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51939 Genomic RNA. Translation: CAA36202.1. Sequence problems.
X73559 Genomic RNA. No translation available.
AF029248 Genomic RNA. Translation: AAB86818.1. Sequence problems.
AF029248 Genomic RNA. Translation: AAB86820.1. Sequence problems.
M27198 Genomic RNA. Translation: AAA74011.1.
PIRiA32440.
S15760.
RefSeqiNP_045299.1. NC_001846.1.

Genome annotation databases

GeneIDi1489749.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51939 Genomic RNA. Translation: CAA36202.1. Sequence problems.
X73559 Genomic RNA. No translation available.
AF029248 Genomic RNA. Translation: AAB86818.1. Sequence problems.
AF029248 Genomic RNA. Translation: AAB86820.1. Sequence problems.
M27198 Genomic RNA. Translation: AAA74011.1.
PIRiA32440.
S15760.
RefSeqiNP_045299.1. NC_001846.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GTHX-ray2.70A6504-6872[»]
2GTIX-ray2.15A6504-6872[»]
3VC8X-ray2.00A/B3245-3333[»]
3VCBX-ray2.40A/B3245-3333[»]
4YPTX-ray2.60A1525-1911[»]
ProteinModelPortaliP0C6X9.
SMRiP0C6X9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1489749.

Miscellaneous databases

EvolutionaryTraceiP0C6X9.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR022570. B-CoV_NSP1.
IPR032505. Corona_NSP4_C.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR032592. NAR_dom.
IPR009466. NSP11.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR002705. Pept_C30/C16_B_coronavir.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR009003. Peptidase_S1_PA.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF16348. Corona_NSP4_C. 1 hit.
PF06478. Corona_RPol_N. 1 hit.
PF11963. DUF3477. 2 hits.
PF01661. Macro. 1 hit.
PF16251. NAR. 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.
PF01831. Peptidase_C16. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF00680. RdRP_1. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMiSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 2 hits.
PROSITEiPS51653. CV_ZBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiR1AB_CVMA5
AccessioniPrimary (citable) accession number: P0C6X9
Secondary accession number(s): O39225
, O39226, P16342, P19750
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: November 30, 2016
This is version 69 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

3D-structure, Complete proteome, 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.