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P0C6Y0

- R1AB_CVMJH

UniProt

P0C6Y0 - R1AB_CVMJH

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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Murine coronavirus (strain JHM) (MHV-JHM) (Murine hepatitis virus)
Status
Reviewed - 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).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
Sitei247 – 2482Cleavage; by PL1-PROCurated
Sitei832 – 8332Cleavage; by PL1-PROCurated
Active sitei1120 – 11201For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1271 – 12711For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1715 – 17151For PL2-PRO activityPROSITE-ProRule annotation
Active sitei1872 – 18721For PL2-PRO activityPROSITE-ProRule annotation
Sitei2840 – 28412Cleavage; by PL2-PROCurated
Sitei3336 – 33372Cleavage; by 3CL-PROCurated
Active sitei3377 – 33771For 3CL-PRO activityPROSITE-ProRule annotation
Active sitei3481 – 34811For 3CL-PRO activityPROSITE-ProRule annotation
Sitei3639 – 36402Cleavage; by 3CL-PROCurated
Sitei3927 – 39282Cleavage; by 3CL-PROCurated
Sitei4019 – 40202Cleavage; by 3CL-PROCurated
Sitei4213 – 42142Cleavage; by 3CL-PROCurated
Sitei4323 – 43242Cleavage; by 3CL-PROCurated
Sitei4460 – 44612Cleavage; by 3CL-PROCurated
Sitei5388 – 53892Cleavage; by 3CL-PROCurated
Sitei5988 – 59892Cleavage; by 3CL-PROCurated
Sitei6507 – 65082Cleavage; by 3CL-PROCurated
Sitei6881 – 68822Cleavage; by 3CL-PROCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1197 – 122529C4-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1793 – 182937C4-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4397 – 441317By similarityAdd
BLAST
Zinc fingeri4439 – 445214By similarityAdd
BLAST
Nucleotide bindingi5669 – 56768ATPBy 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

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 JHM) (MHV-JHM) (Murine hepatitis virus)
Taxonomic identifieri11144 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000007193: Genome

Subcellular locationi

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2835 – 28351F → A: No processing between p210 and peptide HD2. 1 Publication
Mutagenesisi2836 – 28361S → A: No effect. 1 Publication
Mutagenesisi2837 – 28371L → A: No effect. 1 Publication
Mutagenesisi2838 – 28381K → A: No effect. 1 Publication
Mutagenesisi2838 – 28381K → N: No effect. 1 Publication
Mutagenesisi2839 – 28391G → A: Partial processing between p210 and peptide HD2. 1 Publication
Mutagenesisi2839 – 28391G → N: No processing between p210 and peptide HD2. 1 Publication
Mutagenesisi2839 – 28391G → V: No processing between p210 and peptide HD2. 1 Publication
Mutagenesisi2840 – 28401G → A: No processing between p210 and peptide HD2. 1 Publication
Mutagenesisi2840 – 28401G → N: No processing between p210 and peptide HD2. 1 Publication
Mutagenesisi2840 – 28401G → V: No processing between p210 and peptide HD2. 1 Publication
Mutagenesisi2841 – 28411A → N: No effect. 1 Publication
Mutagenesisi2842 – 28421V → N or M: No effect. 1 Publication
Mutagenesisi2846 – 28461V → M: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247Host translation inhibitor nsp1By similarityPRO_0000037354Add
BLAST
Chaini248 – 832585Non-structural protein 2By similarityPRO_0000037355Add
BLAST
Chaini833 – 28402008Papain-like proteinaseBy similarityPRO_0000037356Add
BLAST
Chaini2841 – 3336496Non-structural protein 4By similarityPRO_0000037357Add
BLAST
Chaini3337 – 36393033C-like proteinaseBy similarityPRO_0000037358Add
BLAST
Chaini3640 – 3927288Non-structural protein 6By similarityPRO_0000037359Add
BLAST
Chaini3928 – 401992Non-structural protein 7By similarityPRO_0000037360Add
BLAST
Chaini4020 – 4213194Non-structural protein 8By similarityPRO_0000037361Add
BLAST
Chaini4214 – 4323110Non-structural protein 9By similarityPRO_0000037362Add
BLAST
Chaini4324 – 4460137Non-structural protein 10By similarityPRO_0000037363Add
BLAST
Chaini4461 – 5388928RNA-directed RNA polymeraseBy similarityPRO_0000037364Add
BLAST
Chaini5389 – 5988600HelicaseBy similarityPRO_0000037365Add
BLAST
Chaini5989 – 6507519Guanine-N7 methyltransferaseBy similarityPRO_0000037366Add
BLAST
Chaini6508 – 6881374Uridylate-specific endoribonucleaseBy similarityPRO_0000037367Add
BLAST
Chaini6882 – 71802992'-O-methyl transferaseBy similarityPRO_0000037368Add
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

ProteinModelPortaliP0C6Y0.
SMRiP0C6Y0. Positions 4055-4205, 4329-4453, 6508-6876.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2228 – 224821HelicalSequence AnalysisAdd
BLAST
Transmembranei2289 – 230921HelicalSequence AnalysisAdd
BLAST
Transmembranei2320 – 234021HelicalSequence AnalysisAdd
BLAST
Transmembranei2403 – 242321HelicalSequence AnalysisAdd
BLAST
Transmembranei2445 – 246521HelicalSequence AnalysisAdd
BLAST
Transmembranei2846 – 286621HelicalSequence AnalysisAdd
BLAST
Transmembranei3099 – 311921HelicalSequence AnalysisAdd
BLAST
Transmembranei3121 – 314121HelicalSequence AnalysisAdd
BLAST
Transmembranei3153 – 317321HelicalSequence AnalysisAdd
BLAST
Transmembranei3180 – 320021HelicalSequence AnalysisAdd
BLAST
Transmembranei3205 – 322521HelicalSequence AnalysisAdd
BLAST
Transmembranei3648 – 366821HelicalSequence AnalysisAdd
BLAST
Transmembranei3678 – 369821HelicalSequence AnalysisAdd
BLAST
Transmembranei3705 – 372521HelicalSequence AnalysisAdd
BLAST
Transmembranei3748 – 376821HelicalSequence AnalysisAdd
BLAST
Transmembranei3775 – 379521HelicalSequence AnalysisAdd
BLAST
Transmembranei3802 – 382221HelicalSequence AnalysisAdd
BLAST
Transmembranei3846 – 386621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1083 – 1320238Peptidase C16 1PROSITE-ProRule annotationAdd
BLAST
Domaini1321 – 1481161MacroPROSITE-ProRule annotationAdd
BLAST
Domaini1677 – 1936260Peptidase C16 2PROSITE-ProRule annotationAdd
BLAST
Domaini3337 – 3639303Peptidase C30PROSITE-ProRule annotationAdd
BLAST
Domaini5068 – 5230163RdRp catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini5389 – 547284CV MBDAdd
BLAST
Domaini5644 – 5825182(+)RNA virus helicase ATP-bindingAdd
BLAST
Domaini5826 – 6003178(+)RNA virus helicase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2228 – 2465238HD1Add
BLAST
Regioni2846 – 3225380HD2Add
BLAST
Regioni3648 – 3866219HD3Add
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.

Sequence similaritiesi

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1197 – 122529C4-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1793 – 182937C4-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4397 – 441317By similarityAdd
BLAST
Zinc fingeri4439 – 445214By 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.
IPR022570. Coronavirus_NSP1.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_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.
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.
PF11963. DUF3477. 2 hits.
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.
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_MBD. 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. Align

Isoform Replicase polyprotein 1ab (identifier: P0C6Y0-1) [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
MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK
60 70 80 90 100
GKTLVNHVRV DCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG
110 120 130 140 150
SAVLVKPSKR LSVQAWAKLG VLPKTPAMGL FKRFCLCNTR ECVCDAHVAF
160 170 180 190 200
QLFTVQPDGV CLGNGRFIGW FVPVTAIPEY AKQWLQPWSI LLRKGGNKGS
210 220 230 240 250
VTSGHFRRAV TMPVYDFNVE DACEEVHLNP RGKYSCKAYA LLRGYRGVKP
260 270 280 290 300
ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELSPVWRDS LDNEVVVAWH
310 320 330 340 350
VDRDPRAVMR LQTLATVRSI EYVGQPIEDM VDGDVVMREP AHLLAPNAIV
360 370 380 390 400
KRLPRLVETM LYTDSSVTEF CYKTKLCDCG FITQFGYVDC CGDTCGFRGW
410 420 430 440 450
VPGNMMDGFP CPGCCKSYMP WELEAQSSGV IPEGGVLFTQ STDTVNRESF
460 470 480 490 500
KLYGHAVVPF GGAAYWSPYP GMWLPVIWSS VKSYSYLTYT GVVGCKAIVQ
510 520 530 540 550
ETDAICRFLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN RGDYSLLLEN
560 570 580 590 600
VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSLMVN
610 620 630 640 650
FSREVVDMCM DMALLFMHDV KVATKYVKKV TGKVAVRFKA LGIAVVRKIT
660 670 680 690 700
EWFDLAVDTA ASAAGWLCYQ LVNGLFAVAN GVITFIQEVP ELVKNFVDKF
710 720 730 740 750
KTFFKVLIDS MSVSILSGLT VVKTASNRVC LAGSKVYEVV QKSLPAYIMP
760 770 780 790 800
VGCSEATCLV GEIEPAVFED DVVDVVKAPL TYQGCCKPPS SFEKICIVDK
810 820 830 840 850
LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVVFND KPKVKEVPST
860 870 880 890 900
RKIKIIFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC
910 920 930 940 950
KEHGVIGTKV CALLERLVDD YVYLFDEGGE EVIASRMYCS FSAPDEDCVA
960 970 980 990 1000
TDVVYADENQ DDDADDPVVL VADTQEEDGV AREQVDSADS EICVAHTGGQ
1010 1020 1030 1040 1050
EMTEPDVVGS QTPIASAEET EVGEACDREG IAEVKATVCA DALDACPDQV
1060 1070 1080 1090 1100
EAFDIEKVED SILSELQTEL NAPADKTYED VLAFDAIYSE TLSAFYAVPS
1110 1120 1130 1140 1150
DETHFKVCGF YSPAIERTNC WLRSTLIVMQ SLPLEFKDLG MQKLWLSYKA
1160 1170 1180 1190 1200
GYDQCFVDKL VKSAPKSIIL PQGGYVADFA YFFLSQCSFK VHANWRCLKC
1210 1220 1230 1240 1250
GMELKLQGLD AVFFYGDVVS HMCKCGNSMT LLSADIPYTF DFGVRDDKFC
1260 1270 1280 1290 1300
AFYTPRKVFR AACAVDVNDC HSMAVVDGKQ IDGKVVTKFN GDKFDFMVGH
1310 1320 1330 1340 1350
GMTFSMSPFE IAQLYGSCIT PNVCFVKGDV IKVLRRVGAE VIVNPANGRM
1360 1370 1380 1390 1400
AHGAGVAGAI AKAAGKAFIN ETADMVKAQG VCQVGGCYES TGGKLCKKVL
1410 1420 1430 1440 1450
NIVGPDARGH GNECYSLLER AYQHINKCDN VVTTLISAGI FSVPTDVSLT
1460 1470 1480 1490 1500
YLLGVVTKNV ILVSNNQDDF DVIEKCQVTS VAGTKALSFQ LAKNLCRDVK
1510 1520 1530 1540 1550
FVTNACSSLF SESSFVSSYD VLQEVEALRH DIQLDDDARV FVQANMDCLP
1560 1570 1580 1590 1600
TDWRLVNKFD SVDGVRTIKY FECPGEVFVS SQGKKFGYVQ NGSFKEASVS
1610 1620 1630 1640 1650
QIRALLANKV DVLCTVDGVN FRSCCVAEGE VFGKTLGSVF CDGINVTKVR
1660 1670 1680 1690 1700
CSAIHKGKVF FQYSGLSAAD LAAVKDAFGF DEPQLLQYYS MLGMCKWPVV
1710 1720 1730 1740 1750
VCGNYFAFKQ SNNNCYINVA CLMLQHLSLK FPKWQWRRPG NEFRSGKPLR
1760 1770 1780 1790 1800
FVSLVLAKGS FKFNEPSDST DFIRVELREA DLSGATCDLE FICKCGVKQE
1810 1820 1830 1840 1850
QRKGVDAVMH FGTLDKSGLV KGYNIACTCG DKLVHCTQFN VPFLICSNTP
1860 1870 1880 1890 1900
EGKKLPDDVV AANIFTGGSV GHYTHVKCKP KYQLYDACNV SKVSEAKGNF
1910 1920 1930 1940 1950
TDCLYLKNLK QTFSSVLTTY YLDDVKCVAY KPDLSQYYCE SGKYYTKPII
1960 1970 1980 1990 2000
KAQFRTFEKV EGVYTNFKLV GHDIAEKLNA KLGFDCNSPF MEYKITEWPT
2010 2020 2030 2040 2050
ATGDVVLASD DLYVSRYSGG CVTFGKPVIW RGHEEASLKS LTYFNRPSVV
2060 2070 2080 2090 2100
CENKFNVLPV DVSEPTDRRP VPSAVLVTGA ASGADASAIS TEPGTAKEQK
2110 2120 2130 2140 2150
ACASDSVEDQ IVMEAQKKSS VTTVAVKEVK LNGVKKPVKW NCSVVVNDPT
2160 2170 2180 2190 2200
SETKVVKSLS IVDVYDMFLT GCRYVVWTAN ELSRLINSPT VREYVKWGMS
2210 2220 2230 2240 2250
KLIIPANLLL LRDEKQEFVA PKVVKAKAIA CYGAVKWFLL YCFSWIKFNT
2260 2270 2280 2290 2300
DNKVIYTTEV ASKLTFKLCC LAFKNALQTF NWSVVSRGFF LVATVFLLWF
2310 2320 2330 2340 2350
NFLYANVILS DFYLPNIGPL PMFVGQIVAW VKTTFGVLTI CDFYQVTDLG
2360 2370 2380 2390 2400
YRSSFCNGSM VCELCFSGFD MLDNYESINV VQHVVDRRVS FDYISLFKLV
2410 2420 2430 2440 2450
VELVIGYSLY TVCFYPLFVL VGMQLLTTWL PEFFMLGTMH WSARLFVFVA
2460 2470 2480 2490 2500
NMLPAFTLLR FYIVVTAMYK VYCLCRHVMY GCSKPGCLFC YKRNRSVRVK
2510 2520 2530 2540 2550
CSTVVGGSLR YYDVMANGGT GFCTKHQWNC LNCNSWKPGN TFITHEAAAD
2560 2570 2580 2590 2600
LSKELKRPVN PTDSAYYSVI EVKQVGCSMR LFYERDGQRV YDDVSASLFV
2610 2620 2630 2640 2650
DMNGLLHSKV KGVPETHVVV VENEADKAGF LNAAVFYAQS LYRPMLMVEK
2660 2670 2680 2690 2700
KLITTANTGL SVSRTMFDLY VYSLLRHLDV DRKSLTSFVN AAHNSLKEGV
2710 2720 2730 2740 2750
QLEQVMDTFV GCARRKCAID SDVETKSITK SVMAAVNAGV EVTDESCNNL
2760 2770 2780 2790 2800
VPTYVKSDTI VAADLGVLIQ NNAKHVQSNV AKAANVACIW SVDAFNQLSA
2810 2820 2830 2840 2850
DLQHRLRKAC VKTGLKIKLT YNKQEANVPI LTTPFSLKGG AVFSRVLQWL
2860 2870 2880 2890 2900
FVANLICFIV LWALMPTYAV HKSDMQLPLY ASFKVIDNGV LRDVSVTDAC
2910 2920 2930 2940 2950
FANKFNQFDQ WYESTFGLVY YRNSKACPVV VAVIDQDIGH TLFNVPTKVL
2960 2970 2980 2990 3000
RYGFHVLHFI THAFATDRVQ CYTPHMQIPY DNFYASGCVL SSLCTMLAHA
3010 3020 3030 3040 3050
DGTPHPYCYT EGVMHNASLY SSLVPHVRYN LASSNGYIRF PEVVSEGIVR
3060 3070 3080 3090 3100
VVRTRSMTYC RVGLCEEAEE GICFNFNSSW VLNNPYYRAM PGTFCGRNAF
3110 3120 3130 3140 3150
DLIHQVLGGL VQPIDFFALT ASSVAGAILA IIVVLAFYYL IKLKRAFGDY
3160 3170 3180 3190 3200
TSVVVINVIV WCINFLMLFV FQVYPTLSCL YACFYFYTTL YFPSEISVVM
3210 3220 3230 3240 3250
HLQWLVMYGA IMPLWFCITY VAVVVSNHAL WLFSYCRKIG TDVRSDGTFE
3260 3270 3280 3290 3300
EMALTTFMIT KESYCKLKNS VSDVAFNRYL SLYNKYRYFS GKMDTATYRE
3310 3320 3330 3340 3350
AACSQLAKAM ETFNHNNGND VLYQPPTASV TTSFLQSGIV KMVSPTSKVE
3360 3370 3380 3390 3400
PCVVSVTYGN MTLNGLWLDD KVYCPRHVIC SSADMTDPDY PNLLCRVTSS
3410 3420 3430 3440 3450
DFCVMSDRMS LTVMSYQMQG SLLVLTVTLQ NPNTPKYSFG VVKPGETFTV
3460 3470 3480 3490 3500
LAAYNGRPQG AFHVVMRSSH TIKGSFLCGS CGSVGYVLTG DSVRFVYMHQ
3510 3520 3530 3540 3550
LELSTGCHTG TDFSGNFYGP YRDAQVVQLP VQDYTQTVNV VAWLYAAILN
3560 3570 3580 3590 3600
RCNWFVQSDS CSLEEFNVWA MTNGFSSIKA DLVLDALASM TGVTVEQVLA
3610 3620 3630 3640 3650
AIKRLHSGFQ GKQILGSCVL EDELTPSDVY QQLAGVKLQS KRTRVIKGTC
3660 3670 3680 3690 3700
CWILASTFLF CSIISAFVKW TMFMYVTTHM LGVTLCALCF VIFAMLLIKH
3710 3720 3730 3740 3750
KHLYLTMYIM PVLCTLFYTN YLVVGYKQSF RGLAYAWLSY FVPAVDYTYM
3760 3770 3780 3790 3800
DEVLYGVVLL VAMVFVTMRS INHDVFSTMF LVGRLVSLVS MWYFGANLEE
3810 3820 3830 3840 3850
EVLLFLTSLF GTYTWTTMLS LATAKVIAKW LAVNVLYFTD IPQIKLVLLS
3860 3870 3880 3890 3900
YLCIGYVCCC YWGVLSLLNS IFRMPLGVYN YKISVQELRY MNANGLRPPR
3910 3920 3930 3940 3950
NSFEALMLNF KLLGIGGVPV IEVSQIQSRL TDVKCANVVL LNCLQHLHIA
3960 3970 3980 3990 4000
SNSKLWQYCS TLHNEILATS DLSVAFDKLA QLLVVLFANP AAVDSKCLAS
4010 4020 4030 4040 4050
IEEVSDDYVR DNTVLQALQS EFVNMASFVE YELAKKNLDE AKASGSANQQ
4060 4070 4080 4090 4100
QIKQLEKACN IAKSAYERDR AVARKLERMA DLALTNMYKE ARINDKKSKV
4110 4120 4130 4140 4150
VSALQTMLFS MVRKLDNQAL NSILDNAVKG CVPLNAIPPL TSNTLTIIVP
4160 4170 4180 4190 4200
DKQVFDQVVD NVYVTYAPNV WHIQSIQDAD GAVKQLNEID VNSTWPLVIS
4210 4220 4230 4240 4250
ANRHNEVSTV VLQNNELMPQ KLRTQVVNSG SDMNCNIPTQ CYYNTTGTGK
4260 4270 4280 4290 4300
IVYAILSDCD GLKYTKIVKE DGNCVVLELD PPCKFSVQDV KGLKIKYLYF
4310 4320 4330 4340 4350
VKGCNTLARG WVVGTLSSTV RLQAGTATEY ASNSAILSLC AFSVDPKKTY
4360 4370 4380 4390 4400
LDYIQQGGVP VTNCVKMLCD HAGTGMAITI KPEATTNQDS YGGASVCIYC
4410 4420 4430 4440 4450
RSRVEHPDVD GLCKLRGKFV QVPLGIKDPV SYVLTHDVCQ VCGFWRDGSC
4460 4470 4480 4490 4500
SCVGTGSQFQ SKDTNFLNRV RGTSVNARLV PCASGLDTDV QLRAFDICNA
4510 4520 4530 4540 4550
NRAGIGLYYK VNCFRFQRVD EEGNKLDKFF VVKRTNLEVY NKEKECYELT
4560 4570 4580 4590 4600
KDCGVVAEHE FFTFDVEGSR VPHIVRKDLS KFTMLDLCYA LRHFDRNDCS
4610 4620 4630 4640 4650
TLKEILLTYA ECDESYFQKK DWYDFVENPD IINVYKKLGP IFNRALLNTA
4660 4670 4680 4690 4700
NFADTLVEAG LVGVLTLDNQ DLYGQWYDFG DFVKTVPCCG VAVADSYYSY
4710 4720 4730 4740 4750
MMPMLTMCHA LDSELFVNGT YREFDLVQYD FTDFKLELFN KYFKHWSMTY
4760 4770 4780 4790 4800
HPNTSECEDD RCIIHCANFN ILFSMVLPKT CFGPLVRQIF VDGVPFVVSI
4810 4820 4830 4840 4850
GYHYKELGVV MNMDVDTHRY RLSLKDLLLY AADPALHVAS ASALLDLRTC
4860 4870 4880 4890 4900
CFSVAAITSG VKFQTVKPGN FNQDFYEFIL SKGLLKEGSS VDLKHFFFTQ
4910 4920 4930 4940 4950
DGNAAITDYN YYKYNLPTMV DIKQLLFVVE VVNKYFEIYE GGCIPATQVI
4960 4970 4980 4990 5000
VNNYDKSAGY PFNKFGKARL YYEALSFEEQ DEIYAYTKRN VLPTLTQMNL
5010 5020 5030 5040 5050
KYAISAKNRA RTVAGVSILS TMTGRMFHQK CLKSIAATRG VPVVIGTTKF
5060 5070 5080 5090 5100
YGGWDDMLRR LIKDVDSPVL MGWDYPKCDR AMPNILRIVS SLVLARKHDS
5110 5120 5130 5140 5150
CCSHTDRFYR LANECAQVLG EIVMCGGCYY VKPGGTSSGD ATTAFANSVF
5160 5170 5180 5190 5200
NICQAVSANV CSLMACNGHK IEDLSIRELQ KRLYSNVYRA DHVDPAFVSE
5210 5220 5230 5240 5250
YYEFLNKHFS MIILSDDGVV CYNSEFASKG YIANISDFQQ VLYYQNNVFM
5260 5270 5280 5290 5300
SEAKCWVETD IEKGPHEFCS QHTMLVKMDG DEVYLPYPDP SRILGAGCFV
5310 5320 5330 5340 5350
DDLLKTDSVL LIERFVSLAI DAYPLVYHEN PEYQNVFRVY LEYIKKLYND
5360 5370 5380 5390 5400
LGNQILDSIS VILSTCDGQK FTDETFYKNM YLRSAVMQSV GACVVCSSQT
5410 5420 5430 5440 5450
SLRCGSCIRK PLLCCKCAYD HVMSTDHKYV LSVSPYVCNS PGCDVNDVTK
5460 5470 5480 5490 5500
LYLGGMSYYC EAHKPQYSFK LVMNGMVFGL YKQSCTGSPY IEDFNKIASC
5510 5520 5530 5540 5550
KWTEVDDYVL ANECTERLKL FAAETQKATE EAFKQCYASA TIREIVSDRE
5560 5570 5580 5590 5600
LILSWEIGKV RPPLNKNYVF TGYHFTNNGK TVLGEYVFDK SELTNGVYYR
5610 5620 5630 5640 5650
ATTTYKLSVG DVFILTSHAV SSLSAPTLVP QENYTSVRFA SAYSVPETFQ
5660 5670 5680 5690 5700
NNVPNYQHIG IKRYCTVQGP PGTGKSHLAI GHAVYYCTAR VVYTAASHAA
5710 5720 5730 5740 5750
VDALCEKAHK FLNINDCARI VPAKLRVDCY DKFNVNDTTR KYVFTTINAL
5760 5770 5780 5790 5800
PELVTDIIVV DEVSMLTNYE LSVINSRVRA KHYVYIGDPA QLPAPRVLLN
5810 5820 5830 5840 5850
KGTLEPRYFN SVTKLMCCLG PDIFLGTCYR CPKEIVDTVS ALVYNNKLKA
5860 5870 5880 5890 5900
KNDNSAMCFK VYYKGQTTHE SSSAVNMQQI HLISKLLKAN PSWSNAVFIS
5910 5920 5930 5940 5950
PYNSQNYVAK RVLGLQTQTA DSAQGSAYDF VIYSQTAQTA HSVNVNRFNV
5960 5970 5980 5990 6000
AITRAKKGIL CVMSSMQLIG VFNFTTLTLD KINNPRLQCT TNLFKDCSKS
6010 6020 6030 6040 6050
YVGIPPCAFL LAVDDKYKVS GNLAVCLNVA DSAVTYSRLI SLMGFKLDLT
6060 6070 6080 6090 6100
LDGYCKLFIT RDEAIKRVRA WVGFDAEGAH ATRDSIGTNF PLQLGFSTGI
6110 6120 6130 6140 6150
DFVVEATGMF AERDGYVFKK AAARAPPGEQ FKHLVPLMSR GQKWDVVRIR
6160 6170 6180 6190 6200
IVQMLSDHLV DLADSVVLVT WAASFELTCL RYFAKVGKEV VCSVCNKRAT
6210 6220 6230 6240 6250
CFNSRTGYYG CWRHSYSCDY LYNPLIVDIQ QWGYTGSLTS NHDPICSVHK
6260 6270 6280 6290 6300
GAHVASSDAI MTRCLAVHDC FCKSVNWNLE YPIISNEVSV NTSCRLLQRV
6310 6320 6330 6340 6350
MFRAAMLCNR YDVCYDIGNP KGLACVKGYD FKFYDASPVV KSVKQFVYKY
6360 6370 6380 6390 6400
EAHKDQFLDG LCMFWNCNVD KYPANAVVCR FDTRVLSKLN LPGCNGGSLY
6410 6420 6430 6440 6450
VNKHAFHTNP FTRAAFENLK PMPFFYYSDT PCVYMEGMES KQVDYVPLRS
6460 6470 6480 6490 6500
ATCITRCNLG GAVCLKHAEE YREYLESYNT ATTAGFTFWV YKTFDFYNLW
6510 6520 6530 6540 6550
NTFTRLQSLE NVVYNLVNAG HFDGRAGELP CAVIGEKVIA KIQNEDVVVF
6560 6570 6580 6590 6600
KNNTPFPTNV AVELFAERSI RPHPELKLFR SSNIHVCWNH VLWDYAKDSV
6610 6620 6630 6640 6650
FCSSTYKVCK YTDLQCIESL NVLFDGRDNG ALEAFKKCRN GVYINTTKIK
6660 6670 6680 6690 6700
SLSMIKGPQR ADLNGVVVEK VGDSDVEFWF AMRRDGDDVI FSRTGSLEPS
6710 6720 6730 6740 6750
HYRSPQGNPG GNRVGDLSGN EALARGTIFT QSRFLSSFSP RSEMEKDFMD
6760 6770 6780 6790 6800
LDEDVFIAKY SLQDYAFEHV VYGSFNQKII GGLHLLIGLA RRPKKSNLVI
6810 6820 6830 6840 6850
QEFVPYDSSI HSYFITDENS GSSESVCTVI DLLLDDFVDI VKSLNLKCVS
6860 6870 6880 6890 6900
KVVNVNVDFK DFQFMLWCNE EKVMTFYPRL QAAADWKPGY VMPVLYKYLE
6910 6920 6930 6940 6950
SPMERVNLWN YGKPITLPTG CMMNVAKYTQ LCQYLSTTTL AVPANMRVLH
6960 6970 6980 6990 7000
LGAGSDKGVA PGSAVLRQWL PSGSILVDND MNPFVSDSVA SYYGNCITLP
7010 7020 7030 7040 7050
FDCQWDLIIS DMYDPLTKNI GEYNVSKDGF FTYLCHLIRD KLALGGSVAI
7060 7070 7080 7090 7100
KITEFSWNAE LYSLMGKFAF WTIFCTNVNA SSSEGFLIGI NWLNRTRNEI
7110 7120 7130 7140 7150
DGKTMHANYL FWRNSTMWNG GAYSLFDMTK FPLKAAGTAV VSLKPDQIND
7160 7170 7180
LVLSLIEKGK LLVRDTRKEV FVGDSLVNVK

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

Length:7,180
Mass (Da):803,440
Last modified:June 10, 2008 - v1
Checksum:i313A78E1CC87B347
GO
Isoform Replicase polyprotein 1a (identifier: P0C6V1-1) [UniParc]FASTAAdd to Basket

Also known as: pp1a, ORF1a polyprotein

The sequence of this isoform can be found in the external entry P0C6V1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Length:4,474
Mass (Da):497,595
GO

Sequence cautioni

The sequence AAA46457.1 differs from that shown. Reason: Frameshift at positions 690, 915, 1529, 2069 and 3316.
The sequence AAA46457.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence AAA46458.2 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55148 Genomic RNA. Translation: AAA46457.1. Sequence problems.
M55148 Genomic RNA. Translation: AAA46458.2. Sequence problems.
M18040 Genomic RNA. Translation: AAA46466.1.
S51684 Genomic RNA. Translation: AAB19566.1.
PIRiA36815. RRIHM2.
B36815. VFIHJH.
RefSeqiYP_209229.2. AC_000192.1. [P0C6Y0-1]

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55148 Genomic RNA. Translation: AAA46457.1 . Sequence problems.
M55148 Genomic RNA. Translation: AAA46458.2 . Sequence problems.
M18040 Genomic RNA. Translation: AAA46466.1 .
S51684 Genomic RNA. Translation: AAB19566.1 .
PIRi A36815. RRIHM2.
B36815. VFIHJH.
RefSeqi YP_209229.2. AC_000192.1. [P0C6Y0-1 ]

3D structure databases

ProteinModelPortali P0C6Y0.
SMRi P0C6Y0. Positions 4055-4205, 4329-4453, 6508-6876.
ModBasei Search...
MobiDBi Search...

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.
IPR022570. Coronavirus_NSP1.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_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.
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.
PF11963. DUF3477. 2 hits.
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.
PF01831. Peptidase_C16. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF00680. RdRP_1. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view ]
SMARTi SM00506. A1pp. 1 hit.
[Graphical view ]
SUPFAMi SSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 2 hits.
PROSITEi PS51653. CV_MBD. 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 ]
ProtoNeti Search...

Publicationsi

  1. "The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase."
    Lee H.-J., Shieh C.-K., Gorbalenya A.E., Koonin E.V., la Monica N., Tuler J., Bagdzhardzhyan A., Lai M.M.C.
    Virology 180:567-582(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Sequence and translation of the murine coronavirus 5'-end genomic RNA reveals the N-terminal structure of the putative RNA polymerase."
    Soe L.H., Shieh C.-K., Baker S.C., Chang M.F., Lai M.M.C.
    J. Virol. 61:3968-3976(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-595.
  3. "Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: heterogeneity among MHV strains."
    Bonilla P.J., Gorbalenya A.E., Weiss S.R.
    Virology 198:736-740(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "Murine coronavirus gene 1 polyprotein contains an autoproteolytic activity."
    Baker S.C., La Monica N., Shieh C.K., Lai M.M.
    Adv. Exp. Med. Biol. 276:283-289(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1021-1326.
  5. "Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2."
    Kanjanahaluethai A., Jukneliene D., Baker S.C.
    J. Virol. 77:7376-7382(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF PHE-2835; SER-2836; LEU-2837; LYS-2838; GLY-2839; GLY-2840; ALA-2841; VAL-2842 AND VAL-2846.
  6. "Processing of the coronavirus MHV-JHM polymerase polyprotein: identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a."
    Schiller J.J., Kanjanahaluethai A., Baker S.C.
    Virology 242:288-302(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, SUBCELLULAR LOCATION.
  7. "Conservation of substrate specificities among coronavirus main proteases."
    Hegyi A., Ziebuhr J.
    J. Gen. Virol. 83:595-599(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.

Entry informationi

Entry nameiR1AB_CVMJH
AccessioniPrimary (citable) accession number: P0C6Y0
Secondary accession number(s): P19751
, P29982, Q66194, Q90045
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