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P0C6X6

- R1AB_CVHOC

UniProt

P0C6X6 - R1AB_CVHOC

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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Human coronavirus OC43 (HCoV-OC43)
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
Sitei246 – 2472Cleavage; by PL1-PROBy similarity
Sitei851 – 8522Cleavage; by PL1-PROBy similarity
Active sitei1074 – 10741For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1225 – 12251For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1671 – 16711For PL2-PRO activityPROSITE-ProRule annotation
Active sitei1828 – 18281For PL2-PRO activityPROSITE-ProRule annotation
Sitei2750 – 27512Cleavage; by PL2-PROBy similarity
Sitei3246 – 32472Cleavage; by 3CL-PROBy similarity
Active sitei3287 – 32871For 3CL-PRO activityPROSITE-ProRule annotation
Active sitei3391 – 33911For 3CL-PRO activityPROSITE-ProRule annotation
Sitei3549 – 35502Cleavage; by 3CL-PROBy similarity
Sitei3836 – 38372Cleavage; by 3CL-PROBy similarity
Sitei3925 – 39262Cleavage; by 3CL-PROBy similarity
Sitei4122 – 41232Cleavage; by 3CL-PROBy similarity
Sitei4232 – 42332Cleavage; by 3CL-PROBy similarity
Sitei4369 – 43702Cleavage; by 3CL-PROBy similarity
Sitei5297 – 52982Cleavage; by 3CL-PROBy similarity
Sitei5900 – 59012Cleavage; by 3CL-PROBy similarity
Sitei6421 – 64222Cleavage; by 3CL-PROBy similarity
Sitei6796 – 67972Cleavage; by 3CL-PROBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1151 – 117929C4-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1749 – 178537C4-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4306 – 432217By similarityAdd
BLAST
Zinc fingeri4348 – 436114By similarityAdd
BLAST
Nucleotide bindingi5578 – 55858ATPBy 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

MEROPSiC16.001.

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
OrganismiHuman coronavirus OC43 (HCoV-OC43)
Taxonomic identifieri31631 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007552: 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246Host translation inhibitor nsp1By similarityPRO_0000283826Add
BLAST
Chaini247 – 851605Non-structural protein 2By similarityPRO_0000283827Add
BLAST
Chaini852 – 27501899Papain-like proteinaseBy similarityPRO_0000283828Add
BLAST
Chaini2751 – 3246496Non-structural protein 4By similarityPRO_0000283829Add
BLAST
Chaini3247 – 35493033C-like proteinaseBy similarityPRO_0000283830Add
BLAST
Chaini3550 – 3836287Non-structural protein 6By similarityPRO_0000283831Add
BLAST
Chaini3837 – 392589Non-structural protein 7By similarityPRO_0000283832Add
BLAST
Chaini3926 – 4122197Non-structural protein 8By similarityPRO_0000283833Add
BLAST
Chaini4123 – 4232110Non-structural protein 9By similarityPRO_0000283834Add
BLAST
Chaini4233 – 4369137Non-structural protein 10By similarityPRO_0000283835Add
BLAST
Chaini4370 – 5297928RNA-directed RNA polymeraseBy similarityPRO_0000037308Add
BLAST
Chaini5298 – 5900603HelicaseBy similarityPRO_0000283836Add
BLAST
Chaini5901 – 6421521Guanine-N7 methyltransferaseBy similarityPRO_0000283837Add
BLAST
Chaini6422 – 6796375Uridylate-specific endoribonucleaseBy similarityPRO_0000283838Add
BLAST
Chaini6797 – 70952992'-O-methyltransferaseBy similarityPRO_0000283839Add
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

ProteinModelPortaliP0C6X6.
SMRiP0C6X6. Positions 3964-4114, 4238-4362, 6422-6791.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2138 – 215821HelicalSequence AnalysisAdd
BLAST
Transmembranei2199 – 221921HelicalSequence AnalysisAdd
BLAST
Transmembranei2221 – 224121HelicalSequence AnalysisAdd
BLAST
Transmembranei2313 – 233321HelicalSequence AnalysisAdd
BLAST
Transmembranei2343 – 236321HelicalSequence AnalysisAdd
BLAST
Transmembranei2365 – 238521HelicalSequence AnalysisAdd
BLAST
Transmembranei2752 – 277221HelicalSequence AnalysisAdd
BLAST
Transmembranei2824 – 284421HelicalSequence AnalysisAdd
BLAST
Transmembranei3009 – 302921HelicalSequence AnalysisAdd
BLAST
Transmembranei3031 – 305121HelicalSequence AnalysisAdd
BLAST
Transmembranei3063 – 308321HelicalSequence AnalysisAdd
BLAST
Transmembranei3090 – 311021HelicalSequence AnalysisAdd
BLAST
Transmembranei3115 – 313521HelicalSequence AnalysisAdd
BLAST
Transmembranei3558 – 357821HelicalSequence AnalysisAdd
BLAST
Transmembranei3588 – 360821HelicalSequence AnalysisAdd
BLAST
Transmembranei3615 – 363521HelicalSequence AnalysisAdd
BLAST
Transmembranei3657 – 367721HelicalSequence AnalysisAdd
BLAST
Transmembranei3684 – 370421HelicalSequence AnalysisAdd
BLAST
Transmembranei3711 – 373121HelicalSequence AnalysisAdd
BLAST
Transmembranei3755 – 377521HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1036 – 1274239Peptidase C16 1PROSITE-ProRule annotationAdd
BLAST
Domaini1275 – 1435161MacroPROSITE-ProRule annotationAdd
BLAST
Domaini1631 – 1892262Peptidase C16 2PROSITE-ProRule annotationAdd
BLAST
Domaini3247 – 3549303Peptidase C30PROSITE-ProRule annotationAdd
BLAST
Domaini4977 – 5139163RdRp catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini5298 – 538184CV MBDAdd
BLAST
Domaini5553 – 5734182(+)RNA virus helicase ATP-bindingAdd
BLAST
Domaini5735 – 5904170(+)RNA virus helicase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2138 – 2385248HD1By similarityAdd
BLAST
Regioni2752 – 3135384HD2By similarityAdd
BLAST
Regioni3319 – 3775457HD3By similarityAdd
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 fingeri1151 – 117929C4-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1749 – 178537C4-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4306 – 432217By similarityAdd
BLAST
Zinc fingeri4348 – 436114By similarityAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
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. 1 hit.
PF01661. Macro. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
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. 1 hit.
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: P0C6X6-1) [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
MSKINKYGLE LHWAPEFPWM FEDAEEKLDN PSSSEVDMIC STTAQKLETD
60 70 80 90 100
GICPENHVMV DCRRLLKQEC CVQSSLIREI VMNASPYHLE VLLQDALQSR
110 120 130 140 150
EAVLVTTPLG MSLEACYVRG CNPKGWTMGL FRRRSVCNTG RCTVNKHVAY
160 170 180 190 200
QLYMIDPAGV CLGAGQFVGW VIPLAFMPVQ SRKFIVPWVM YLRKRGEKGA
210 220 230 240 250
YNKDHGCGGF GHVYDFKVED AYDQVHDEPK GKFSKKAYAL IRGYRGVKPL
260 270 280 290 300
LYVDQYGCDY TGSLADGLEA YADKTLQEMK ALFPTWSQEL PFDVIVAWHV
310 320 330 340 350
VRDPRYVMRL QSAATICSVA YVANPTEDLC DGSVVIKEPV HVYADDSIIL
360 370 380 390 400
RQYNLFDIMS HFYMEADTVV NAFYGVALKD CGFVMQFGYI DCEQDSCDFK
410 420 430 440 450
GWIPGNMIDG FACTTCGHVY EVGDLIAQSS GVLPVNPVLH TKSAAGYGGF
460 470 480 490 500
GCKDSFTLYG QTVVYFGGCV YWSPARNIWI PILKSSVKSY DSLVYTGVLG
510 520 530 540 550
CKAIVKETNL ICKALYLDYV QHKCGNLHQR ELLGVSDVWH KQLLINRGVY
560 570 580 590 600
KPLLENIDYF NMRRAKFSLE TFTVCADGFM PFLLDDLVPR AYYLAVSGQA
610 620 630 640 650
FCDYADKLCH AVVSKSKELL DVSLDSLGAA IHYLNSKIVD LAQHFSDFGT
660 670 680 690 700
SFVSKIVHFF KTFTTSTALA FAWVLFHVLH GAYIVVESDI YFVKNIPRYA
710 720 730 740 750
SAVAQAFQSV AKVVLDSLRV TFIDGLSCFK IGRRRICLSG RKIYEVERGL
760 770 780 790 800
LHSSQLPLDV YDLTMPSQVQ KAKQKPIYLK GSGSDFSLAD SVVEVVTTSL
810 820 830 840 850
TPCGYSEPPK VADKICIVDN VYMAKAGDKY YPVVVDDHVG LLDQAWRVPC
860 870 880 890 900
AGRRVTFKEQ PTVKEIISMP KIIKVFYELD NDFNTILNTA CGVFEVDDTV
910 920 930 940 950
DMEEFYAVVI DAIEEKLSPC KELEGVGAKV SAFLQKLEDN PLFLFDEAGE
960 970 980 990 1000
EVFAPKLYCA FTAPEDDDFL EESDVEEDDV EGEETDLTIT SAGQPCVASE
1010 1020 1030 1040 1050
QEESSEVLED TLDDGPSVET SDSQVEEDVE MSDFVDLESV IQDYENVCFE
1060 1070 1080 1090 1100
FYTTEPEFVK VLGLYVPKAT RNNCWLRSVL AVMQKLPCQF KDKNLQDLWV
1110 1120 1130 1140 1150
LYKQQYSQLF VDTLVNKIPA NIVLPQGGYV ADFAYWFLTL CDWQCVAYWK
1160 1170 1180 1190 1200
CIKCDLALKL KGLDAMFFYG DVVSHICKCG ESMVLIDVDV PFTAHFALKD
1210 1220 1230 1240 1250
KLFCAFITKR IVYKAACVVD VNDSHSMAVV DGKQIDDHRI TSITSDKFDF
1260 1270 1280 1290 1300
IIGHGMSFSM TTFEIAQLYG SCITPNVCFV KGDIIKVSKL VKAEVVVNPA
1310 1320 1330 1340 1350
NGHMVHGGGV AKAIAVAAGQ QFVKETTNMV KSKGVCATGD CYVSTGGKLC
1360 1370 1380 1390 1400
KTVLNVVGPD ARTQGKQSYV LLERVYKHFN NYDCVVTTLI SAGIFSVPSD
1410 1420 1430 1440 1450
VSLTYLLGTA KKQVVLVSNN QEDFDLISKC QITAVEGTKK LAARLSFNVG
1460 1470 1480 1490 1500
RSIVYETDAN KLILINDVAF VSTFNVLQDV LSLRHDIALD DDARTFVQSN
1510 1520 1530 1540 1550
VDVLPEGWRV VNKFYQINGV RTVKYFECTG GIDICSQDKV FGYVQQGIFN
1560 1570 1580 1590 1600
KATVAQIKAL FLDKVDILLT VDGVNFTNRF VPVGESFGKS LGNVFCDGVN
1610 1620 1630 1640 1650
VTKHKCDINY KGKVFFQFDN LSSEDLKAVR SSFNFDQKEL LAYYNMLVNC
1660 1670 1680 1690 1700
FKWQVVVNGK YFTFKQANNN CFVNVSCLML QSLHLTFKIV QWQEAWLEFR
1710 1720 1730 1740 1750
SGRPARFVAL VLAKGGFKFG DPADSRDFLR VVFSQVDLTG AICDFEIACK
1760 1770 1780 1790 1800
CGVKQEQRTG LDAVMHFGTL SREDLEIGYT VDCSCGKKLI HCVRFDVPFL
1810 1820 1830 1840 1850
ICSNTPASVK LPKGVGSANI FIGDNVGHYV HVKCEQSYQL YDASNVKKVT
1860 1870 1880 1890 1900
DVTGKLSDCL YLKNLKQTFK SVLTTYYLDD VKKIEYKPDL SQYYCDGGKY
1910 1920 1930 1940 1950
YTQRIIKAQF KTFEKVDGVY TNFKLIGHTV CDSLNSKLGF DSSKEFVEYK
1960 1970 1980 1990 2000
ITEWPTATGD VVLANDDLYV KRYERGCITF GKPVIWLSHE KASLNSLTYF
2010 2020 2030 2040 2050
NRPLLVDDNK FDVLKVDDVD DSGDSSESGA KETKEINIIK LSGVKKPFKV
2060 2070 2080 2090 2100
EDSVIVNDDT SETKYVKSLS IVDVYDMWLT GCKYVVRTAN ALSRAVNVPT
2110 2120 2130 2140 2150
IRKFIKFGMT LVSIPIDLLN LREIKPAVNV VKAVRNKTSA CFNFIKWLFV
2160 2170 2180 2190 2200
LLFGWIKISA DNKVIYTTEI ASKLTCKLVA LAFKNAFLTF KWSMVARGAC
2210 2220 2230 2240 2250
IIATIFLLWF NFIYANVIFS DFYLPKIGFL PTFVGKIAQW IKNTFSLVTI
2260 2270 2280 2290 2300
CDLYSIQDVG FKNQYCNGSI ACQFCLAGFD MLDNYKAIDV VQYEADRRAF
2310 2320 2330 2340 2350
VDYTGVLKIV IELIVSYALY TAWFYPLFAL ISIQILTTWL PELFMLSTLH
2360 2370 2380 2390 2400
WSFRLLVALA NMLPAHVFMR FYIIIASFIK LFSLFKHVAY GCSKSGCLFC
2410 2420 2430 2440 2450
YKRNRSLRVK CSTIVGGMIR YYDVMANGGT GFCSKHQWNC IDCDSYKPGN
2460 2470 2480 2490 2500
TFITVEAALD LSKELKRPIQ PTDVAYHTVT DVKQVGCSMR LFYDRDGQRI
2510 2520 2530 2540 2550
YDDVNASLFV DYSNLLHSKV KSVPNMHVVV VENDADKANF LNAAVFYAQS
2560 2570 2580 2590 2600
LFRPILMVDK NLITTANTGT SVTETMFDVY VDTFLSMFDV DKKSLNALIA
2610 2620 2630 2640 2650
TAHSSIKQGT QIYKVLDTFL SCARKSCSID SDVDTKCLAD SVMSAVSAGL
2660 2670 2680 2690 2700
ELTDESCNNL VPTYLKSDNI VAADLGVLIQ NSAKHVQGNV AKIAGVSCIW
2710 2720 2730 2740 2750
SVDAFNQFSS DFQHKLKKAC CKTGLKLKLT YNKQMANVSV LTTPFSLKGG
2760 2770 2780 2790 2800
AVFSYFVYVC FVLSLVCFIG LWCLMPTYTV HKSDFQLPVY ASYKVLDNGV
2810 2820 2830 2840 2850
IRDVSVEDVC FANKFEQFDQ WYESTFGLSY YSNSMACPIV VAVIDQDFGS
2860 2870 2880 2890 2900
TVFNVPTKVL RYGYHVLHFI THALSADGVQ CYTPHSQISY SNFYASGCVL
2910 2920 2930 2940 2950
SSACTMFTMA DGSPQPYCYT DGLMQNASLY SSLVPHVRYN LANAKGFIRF
2960 2970 2980 2990 3000
PEVLREGLVR VVRTRSMSYC RVGLCEEADE GICFNFNGSW VLNNDYYRSL
3010 3020 3030 3040 3050
PGTFCGRDVF DLIYQLFKGL AQPVDFLALT ASSIAGAILA VIVVLVFYYL
3060 3070 3080 3090 3100
IKLKRAFGDY TSVVFVNVIV WCVNFMMLFV FQVYPTLSCV YAICYFYATL
3110 3120 3130 3140 3150
YFPSEISVIM HLQWLVMYGT IMPLWFCLLY IAVVVSNHAF WVFSYCRKLG
3160 3170 3180 3190 3200
TSVRSDGTFE EMALTTFMIT KDSYCKLKNS LSDVAFNRYL SLYNKYRYYS
3210 3220 3230 3240 3250
GKMDTAAYRE AACSQLAKAM DTFTNNNGSD VLYQPPTASV STSFLQSGIV
3260 3270 3280 3290 3300
KMVNPTSKVE PCVVSVTYGN MTLNGLWLDD KVYCPRHVIC SASDMTNPDY
3310 3320 3330 3340 3350
TNLLCRVTSS DFTVLFDRLS LTVMSYQMRG CMLVLTVTLQ NSRTPKYTFG
3360 3370 3380 3390 3400
VVKPGETFTV LAAYNGKPQG AFHVTMRSSY TIKGSFLCGS CGSVGYVIMG
3410 3420 3430 3440 3450
DCVKFVYMHQ LELSTGCHTG TDFNGDFYGP YKDAQVVQLP IQDYIQSVNF
3460 3470 3480 3490 3500
LAWLYAAILN NCNWFIQSDK CSVEDFNVWA LSNGFSQVKS DLVIDALASM
3510 3520 3530 3540 3550
TGVSLETLLA AIKRLKNGFQ GRQIMGSCSF EDELTPSDVY QQLAGIKLQS
3560 3570 3580 3590 3600
KRTRLFKGTV CWIMASTFLF SCIITAFVKW TMFMYVTTNM FSITFCALCV
3610 3620 3630 3640 3650
ISLAMLLVKH KHLYLTMYIT PVLFTLLYNN YLVVYKHTFR GYVYAWLSYY
3660 3670 3680 3690 3700
VPSVEYTYTD EVIYGMLLLV GMVFVTLRSI NHDLFSFIMF VGRLISVFSL
3710 3720 3730 3740 3750
WYKGSNLEEE ILLMLASLFG TYTWTTVLSM AVAKVIAKWV AVNVLYFTDI
3760 3770 3780 3790 3800
PQIKIVLLCY LFIGYIISCY WGLFSLMNSL FRMPLGVYNY KISVQELRYM
3810 3820 3830 3840 3850
NANGLRPPKN SFEALMLNFK LLGIGGVPII EVSQFQSKLT DVKCANVVLL
3860 3870 3880 3890 3900
NCLQHLHVAS NSKLWHYCST LHNEILATSD LSVAFEKLAQ LLIVLFANPA
3910 3920 3930 3940 3950
AVDSKCLTSI EEVCDDYAKD NTVLQALQSE FVNMASFVEY EVAKKNLDEA
3960 3970 3980 3990 4000
RFSGSANQQQ LKQLEKACNI AKSAYERDRA VAKKLERMAD LALTNMYKEA
4010 4020 4030 4040 4050
RINDKKSKVV SALQTMLFSM VRKLDNQALN SILDNAVKGC VPLNAIPSLA
4060 4070 4080 4090 4100
ANTLNIIVPD KSVYDQIVDN IYVTYAGNVW QIQTIQDSDG TNKQLNEISD
4110 4120 4130 4140 4150
DCNWPLVIIA NRYNEVSATV LQNNELMPAK LKIQVVNSGP DQTCNTPTQC
4160 4170 4180 4190 4200
YYNNSNNGKI VYAILSDVDG LKYTKILKDD GNFVVLELDP PCKFTVQDAK
4210 4220 4230 4240 4250
GLKIKYLYFV KGCNTLARGW VVGTISSTVR LQAGTATEYA SNSSILSLCA
4260 4270 4280 4290 4300
FSVDPKKTYL DFIQQGGTPI ANCVKMLCDH AGTGMAITVK PDATTSQDSY
4310 4320 4330 4340 4350
GGASVCIYCR ARVEHPDVDG LCKLRGKFVQ VPVGIKDPVS YVLTHDVCRV
4360 4370 4380 4390 4400
CGFWRDGSCS CVSTDTTVQS KDTNFLNRVR GASVDARLVP CASGLSTDVQ
4410 4420 4430 4440 4450
LRAFDIYNAS VAGIGLHLKV NCCRFQRVDE NGDKLDQFFV VKRTDLTIYN
4460 4470 4480 4490 4500
REMKCYERVK DCKFVAEHDF FTFDVEGSRV PHIVRKDLTK YTMLDLCYAL
4510 4520 4530 4540 4550
RHFDRNDCML LCDILSIYAG CEQSYFTKKD WYDFVENPDI INVYKKLGPI
4560 4570 4580 4590 4600
FNRALVSATE FADKLVEVGL VGVLTLDNQD LNGKWYDFGD YVIAAPGCGV
4610 4620 4630 4640 4650
AIADSYYSYI MPMLTMCHAL DCELYVNNAY RLFDLVQYDF TDYKLELFNK
4660 4670 4680 4690 4700
YFKHWSMPYH PNTVDCQDDR CIIHCANFNI LFSMVLPNTC FGPLVRQIFV
4710 4720 4730 4740 4750
DGVPFVVSIG YHYKELGIVM NMDVDTHRYR LSLKDLLLYA ADPALHVASA
4760 4770 4780 4790 4800
SALYDLRTCC FSVAAITSGV KFQTVKPGNF NQDFYDFVLS KGLLKEGSSV
4810 4820 4830 4840 4850
DLKHFFFTQD GNAAITDYNY YKYNLPTMVD IKQLLFVLEV VYKYFEIYDG
4860 4870 4880 4890 4900
GCIPASQVIV NNYDKSAGYP FNKFGKARLY YEALSFEEQD EIYAYTKRNV
4910 4920 4930 4940 4950
LPTLTQMNLK YAISAKNRAR TVAGVSILST MTGRMFHQKC LKSIAATRGV
4960 4970 4980 4990 5000
PVVIGTTKFY GGWDDMLRRL IKDVDNPVLM GWDYPKCDRA MPNILRIVSS
5010 5020 5030 5040 5050
LVLARKHETC CSQSDRFYRL ANECAQVLSE IVMCGGCYYV KPGGTSSGDA
5060 5070 5080 5090 5100
TTAFANSVFN ICQAVSANVC ALMSCNGNKI EDLSIRALQK RLYSHVYRSD
5110 5120 5130 5140 5150
KVDSTFVTEY YEFLNKHFSM MILSDDGVVC YNSDYASKGY IANISAFQQV
5160 5170 5180 5190 5200
LYYQNNVFMS ESKCWVEHDI NNGPHEFCSQ HTMLVKMDGD DVYLPYPNPS
5210 5220 5230 5240 5250
RILGAGCFVD DLLKTDSVLL IERFVSLAID AYPLVYHENE EYQKVFRVYL
5260 5270 5280 5290 5300
AYIKKLYNDL GNQILDSYSV ILSTCDGQKF TDESFYKNMY LRSAVMQSVG
5310 5320 5330 5340 5350
ACVVCSSQTS LRCGSCIRKP LLCCKCCYDH VMATDHKYVL SVSPYVCNAP
5360 5370 5380 5390 5400
GCDVNDVTKL YLGGMSYYCE DHKPQYSFKL VMNGLVFGLY KQSCTGSPYI
5410 5420 5430 5440 5450
DDFNRIASCK WTDVDDYILA NECTERLKLF AAETQKATEE AFKQSYASAT
5460 5470 5480 5490 5500
IQEIVSEREL ILSWEIGKVK PPLNKNYVFT GYHFTKNGKT VLGEYVFDKS
5510 5520 5530 5540 5550
ELTNGVYYRA TTTYKLSVGD VFVLTSHSVA NLSAPTLVPQ ENYSSIRFAS
5560 5570 5580 5590 5600
VYSVLETFQN NVVNYQHIGM KRYCTVQGPP GTGKSHLAIG LAVFYCTARV
5610 5620 5630 5640 5650
VYTAASHAAV DALCEKAYKF LNINDCTRIV PAKVRVECYD KFKINDTTRK
5660 5670 5680 5690 5700
YVFTTINALP EMVTDIVVVD EVSMLTNYEL SVINARIRAK HYVYIGDPAQ
5710 5720 5730 5740 5750
LPAPRVLLSK GTLEPKYFNT VTKLMCCLGP DIFLGTCYRC PKEIVDTVSA
5760 5770 5780 5790 5800
LVYENKLKAK NESSLLCFKV YYKGVTTHES SSAVNMQQIY LINKFLKANP
5810 5820 5830 5840 5850
LWHKAVFISP YNSQNFAAKR VLGLQTQTVD SAQGSEYDYV IYSQTAETAH
5860 5870 5880 5890 5900
SVNVNRFNVA ITRAKKGILC VMSNMQLFEA LQFTTLTLDK VPQAVETKVQ
5910 5920 5930 5940 5950
CSTNLFKDCS KSYSGYHPAH APSFLAVDDK YKATGDLAVC LGIGDSAVTY
5960 5970 5980 5990 6000
SRLISLMGFK LDVTLDGYCK LFITKEEAVK RVRAWVGFDA EGAHATLDSI
6010 6020 6030 6040 6050
GTNFPLQLGF STGIDFVVEA TGLFADRDGY SFKKAVAKAP PGEQFKHLIP
6060 6070 6080 6090 6100
LMTRGHRWDV VRPRIVQMFA DHLIDLSDCV VLVTWAANFE LTCLRYFAKV
6110 6120 6130 6140 6150
GREISCNVCT KRATVYNSRT GYYGCWRHSV TCDYLYNPLI VDIQQWGYIG
6160 6170 6180 6190 6200
SLSSNHDLYC SVHKGAHVAS SDAIMTRCLA VYDCFCNNIN WNVEYPIISN
6210 6220 6230 6240 6250
ELSINTSCRV LQRVILKAAM LCNRYTLCYD IGNPKGIACV KDFDFKFYDA
6260 6270 6280 6290 6300
QPIVKSVKTL LYSFEAHKDS FKDGLCMFWN CNVDKYPPNA VVCRFDTRVL
6310 6320 6330 6340 6350
NNLNLPGCNG GSLYVNKHAF HTKPFARAAF EHLKPMPFFY YSDTPCVYMD
6360 6370 6380 6390 6400
GMDAKQVDYV PLKSATCITR CNLGGAVCLK HAEEYREYLE SYNTATTAGF
6410 6420 6430 6440 6450
TFWVYKTFDF YNLWNTFTKL QSLENVVYNL VKTGHYTGQA GEMPCAIIND
6460 6470 6480 6490 6500
KVVTKIDKED VVIFINNTTY PTNVAVELFA KRSVRHHPEL KLFRNLNIDV
6510 6520 6530 6540 6550
CWKHVIWDYA RESIFCSNTY GVCMYTDLKF IDKLNVLFDG RDNGAFEAFK
6560 6570 6580 6590 6600
RSNNGVYIST TKVKSLSMIR GPPRAELNGV VVDKVGDTDC VFYFAVRKEG
6610 6620 6630 6640 6650
QDVIFSQFDS LGVSSNQSPQ GNLGSNGKPG NVGGNDALSI STIFTQSRVI
6660 6670 6680 6690 6700
SSFTCRTDME KDFIALDQDV FIQKYGLEDY AFEHIVYGNF NQKIIGGLHL
6710 6720 6730 6740 6750
LIGLYRRQQT SNLVVQEFVS YDSSIHSYFI TDEKSGGSKS VCTVIDILLD
6760 6770 6780 6790 6800
DFVTLVKSLN LNCVSKVVNV NVDFKDFQFM LWCNDEKVMT FYPRLQAASD
6810 6820 6830 6840 6850
WKPGYSMPVL YKYLNSPMER VSLWNYGKPV TLPTGCMMNV AKYTQLCQYL
6860 6870 6880 6890 6900
NTTTLAVPVN MRVLHLGAGS EKGVAPGSAV LRQWLPAGTI LVDNDLYPFV
6910 6920 6930 6940 6950
SDSVATYFGD CITLPFDCQW DLIISDMYDP ITKNIGEYNV SKDGFFTYIC
6960 6970 6980 6990 7000
HMIRDKLALG GSVAIKITEF SWNAELYKLM GYFAFWTVFC TNANASSSEG
7010 7020 7030 7040 7050
FLIGINYLCK PKVEIDGNVM HANYLFWRNS TVWNGGAYSL FDMAKFPLKL
7060 7070 7080 7090
AGTAVINLRA DQINDMVYSL LEKGKLLIRD TNKEVFVGDS LVNVI

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

Length:7,095
Mass (Da):797,914
Last modified:June 10, 2008 - v1
Checksum:i157CDEBD4CE45D4A
GO
Isoform Replicase polyprotein 1a (identifier: P0C6U7-1) [UniParc]FASTAAdd to Basket

Also known as: pp1a, ORF1a polyprotein

The sequence of this isoform can be found in the external entry P0C6U7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Length:4,383
Mass (Da):491,305
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti426 – 4261I → M in AAT84359. (PubMed:15650185)Curated
Sequence conflicti426 – 4261I → M in AAT84351. (PubMed:15650185)Curated
Sequence conflicti813 – 8131D → A in AAT84359. (PubMed:15650185)Curated
Sequence conflicti813 – 8131D → A in AAT84351. (PubMed:15650185)Curated
Sequence conflicti4376 – 43772LN → FK in AAR01012. (PubMed:15280490)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881H → D in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti207 – 2071C → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti291 – 2911P → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti317 – 3171C → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti356 – 3561F → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti545 – 5451I → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti762 – 7621D → N in strain: Isolate 87309 Belgium 2003.
Natural varianti953 – 9531F → L in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
Natural varianti989 – 9891I → V in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
Natural varianti1305 – 13051V → A in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
Natural varianti1328 – 13281N → D in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti1379 – 13791F → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti1504 – 15041L → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti1740 – 17401G → E in strain: Isolate 87309 Belgium 2003.
Natural varianti1825 – 18251N → K in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti1936 – 19361S → A in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
Natural varianti1965 – 19651N → T in strain: ATCC VR-759, Isolate clinical OC43-Paris.
Natural varianti2004 – 20041L → S in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
Natural varianti2022 – 20221S → G in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti2138 – 21403TSA → ISV in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti2256 – 22561I → M in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti2257 – 22571Q → H in strain: Isolate 87309 Belgium 2003.
Natural varianti2386 – 23861K → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti2500 – 25001I → T in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
Natural varianti2921 – 29211D → E in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti2961 – 29611V → I in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti3086 – 30861T → I in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti3440 – 34401P → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti3451 – 34511L → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti3466 – 34661I → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti4067 – 40671I → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti4071 – 40711I → V in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
Natural varianti4382 – 43821A → T in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti4994 – 49941I → L in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate Tulsa 1999 and Isolate 87309 Belgium 2003.
Natural varianti5014 – 50152SD → RT in strain: Isolate Tulsa 1999.
Natural varianti5765 – 57651L → S in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
Natural varianti5997 – 59971L → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti6236 – 62361G → A in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti6454 – 64541T → A in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
Natural varianti6546 – 65461F → L in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
Natural varianti6636 – 66361D → E in strain: Isolate 87309 Belgium 2003.
Natural varianti6665 – 66651A → T in strain: Isolate 87309 Belgium 2003.
Natural varianti6754 – 67541T → A in strain: ATCC VR-759 and Isolate clinical OC43-Paris.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY903459 Genomic RNA. Translation: AAX85666.1.
AY903460 Genomic RNA. Translation: AAX85675.1.
AY585228 Genomic RNA. Translation: AAT84351.1.
AY585229 Genomic RNA. Translation: AAT84359.1.
AY391777 Genomic RNA. Translation: AAR01012.1.
AF124989 Genomic RNA. Translation: AAD32993.1.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY903459 Genomic RNA. Translation: AAX85666.1 .
AY903460 Genomic RNA. Translation: AAX85675.1 .
AY585228 Genomic RNA. Translation: AAT84351.1 .
AY585229 Genomic RNA. Translation: AAT84359.1 .
AY391777 Genomic RNA. Translation: AAR01012.1 .
AF124989 Genomic RNA. Translation: AAD32993.1 .

3D structure databases

ProteinModelPortali P0C6X6.
SMRi P0C6X6. Positions 3964-4114, 4238-4362, 6422-6791.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C16.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
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. 1 hit.
PF01661. Macro. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
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. 1 hit.
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. "Circulation of genetically distinct contemporary human coronavirus OC43 strains."
    Vijgen L., Keyaerts E., Lemey P., Moes E., Li S., Vandamme A.M., Van Ranst M.
    Virology 337:85-92(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate 19572 Belgium 2004 and Isolate 87309 Belgium 2003.
  2. "Human respiratory coronavirus OC43: genetic stability and neuroinvasion."
    St Jean J.R., Jacomy H., Desforges M., Vabret A., Freymuth F., Talbot P.J.
    J. Virol. 78:8824-8834(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate ATCC VR-759 and Isolate clinical OC43-Paris.
  3. "Complete genomic sequence of human coronavirus OC43: molecular clock analysis suggests a relatively recent zoonotic coronavirus transmission event."
    Vijgen L., Keyaerts E., Moes E., Thoelen I., Wollants E., Lemey P., Vandamme A.M., Van Ranst M.
    J. Virol. 79:1595-1604(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate ATCC VR-759.
  4. "Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay."
    Stephensen C.B., Casebolt D.B., Gangopadhyay N.N.
    Virus Res. 60:181-189(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4871-5177.
    Strain: Isolate Tulsa 1999.

Entry informationi

Entry nameiR1AB_CVHOC
AccessioniPrimary (citable) accession number: P0C6X6
Secondary accession number(s): Q4VID8
, Q4VIE7, Q696Q1, Q6TNG2, Q9WAC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: October 29, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The sequence shown is that of isolate 19572 Belgium 2004.

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