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P0C6X9

- R1AB_CVMA5

UniProt

P0C6X9 - R1AB_CVMA5

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Protein

Replicase polyprotein 1ab

Gene
rep, 1a-1b
Organism
Murine coronavirus (strain A59) (MHV-A59) (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.
The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 By similarity.
The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function By similarity.
The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) By similarity.
The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction By similarity.
Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter By similarity.
Nsp9 is a ssRNA-binding protein By similarity.
NendoU is a Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond By similarity.
Non-structural protein 1: binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response By similarity.

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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-PRO Inferred
Sitei832 – 8332Cleavage; by PL1-PRO Inferred
Active sitei1121 – 11211For PL1-PRO activity By similarity
Active sitei1272 – 12721For PL1-PRO activity By similarity
Active sitei1716 – 17161For PL2-PRO activity By similarity
Active sitei1873 – 18731For PL2-PRO activity By similarity
Sitei2837 – 28382Cleavage; by PL2-PRO
Sitei3333 – 33342Cleavage; by 3CL-PRO
Active sitei3374 – 33741For 3CL-PRO activity By similarity
Active sitei3478 – 34781For 3CL-PRO activity
Sitei3635 – 36362Cleavage; by 3CL-PRO
Sitei3921 – 39222Cleavage; by 3CL-PRO
Sitei4013 – 40142Cleavage; by 3CL-PRO
Sitei4207 – 42082Cleavage; by 3CL-PRO
Sitei4317 – 43182Cleavage; by 3CL-PRO
Sitei4454 – 44552Cleavage; by 3CL-PRO
Sitei5382 – 53832Cleavage; by 3CL-PRO
Sitei5982 – 59832Cleavage; by 3CL-PRO Inferred
Sitei6503 – 65042Cleavage; by 3CL-PRO Inferred
Sitei6877 – 68782Cleavage; by 3CL-PRO Inferred

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1198 – 122629C4-type 1Add
BLAST
Zinc fingeri1794 – 183037C4-type 2Add
BLAST
Zinc fingeri4391 – 440717 By similarityAdd
BLAST
Zinc fingeri4433 – 444614 By similarityAdd
BLAST
Nucleotide bindingi5663 – 56708ATP By 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 ISG15 activity Source: UniProtKB-KW
  5. suppression by virus of host translation 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, 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:
Non-structural protein 1
Short name:
nsp1
Alternative name(s):
p28
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p65
Alternative name(s):
PL1-PRO/PL2-PRO
PL1/PL2
Papain-like proteinases 1/2
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
Exoribonuclease (EC:3.1.13.-)
Short name:
ExoN
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 positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000007192: Genome

Subcellular locationi

Chain Non-structural protein 3 : Host membrane; Multi-pass membrane protein Reviewed prediction 1 Publication
Chain Non-structural protein 4 : Host membrane; Multi-pass membrane protein Reviewed prediction 1 Publication
Chain Non-structural protein 6 : Host membrane; Multi-pass membrane protein Reviewed prediction 1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
Chain Helicase : Host endoplasmic reticulum-Golgi intermediate compartment Reviewed prediction
Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA.1 Publication
Chain Uridylate-specific endoribonuclease : Host cytoplasmhost perinuclear region By similarity 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2225 – 224521Helical; Reviewed predictionAdd
BLAST
Transmembranei2286 – 230621Helical; Reviewed predictionAdd
BLAST
Transmembranei2314 – 233421Helical; Reviewed predictionAdd
BLAST
Transmembranei2400 – 242021Helical; Reviewed predictionAdd
BLAST
Transmembranei2442 – 246221Helical; Reviewed predictionAdd
BLAST
Transmembranei2625 – 264521Helical; Reviewed predictionAdd
BLAST
Transmembranei2847 – 286721Helical; Reviewed predictionAdd
BLAST
Transmembranei3096 – 311621Helical; Reviewed predictionAdd
BLAST
Transmembranei3118 – 313821Helical; Reviewed predictionAdd
BLAST
Transmembranei3150 – 317021Helical; Reviewed predictionAdd
BLAST
Transmembranei3177 – 319721Helical; Reviewed predictionAdd
BLAST
Transmembranei3202 – 322221Helical; Reviewed predictionAdd
BLAST
Transmembranei3644 – 366421Helical; Reviewed predictionAdd
BLAST
Transmembranei3674 – 369421Helical; Reviewed predictionAdd
BLAST
Transmembranei3699 – 371921Helical; Reviewed predictionAdd
BLAST
Transmembranei3742 – 376221Helical; Reviewed predictionAdd
BLAST
Transmembranei3769 – 378921Helical; Reviewed predictionAdd
BLAST
Transmembranei3796 – 381621Helical; Reviewed predictionAdd
BLAST
Transmembranei3840 – 386021Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. host cell endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  2. host cell membrane Source: UniProtKB-SubCell
  3. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
  4. 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
Mutagenesisi3331 – 33311F → A, H or W: No effect. 1 Publication
Mutagenesisi3332 – 33321L → I or S: No processing between peptide HD2 and 3CL-PRO. 1 Publication
Mutagenesisi3333 – 33331Q → A, K or R: No processing between peptide HD2 and 3CL-PRO. 1 Publication
Mutagenesisi3334 – 33341S → A: No effect. 1 Publication
Mutagenesisi3334 – 33341S → C: No processing between peptide HD2 and 3CL-PRO. 1 Publication
Mutagenesisi3335 – 33351G → A: No effect. 1 Publication
Mutagenesisi3335 – 33351G → P: No processing between peptide HD2 and 3CL-PRO. 1 Publication
Mutagenesisi3336 – 33361I → L: No effect. 1 Publication
Mutagenesisi3478 – 34781C → A: Complete loss of 3CL-PRO activity. 1 Publication
Mutagenesisi5381 – 53811L → I: No processing between RDRP and helicase. 1 Publication
Mutagenesisi5381 – 53811L → M: No effect. 1 Publication
Mutagenesisi5382 – 53821Q → K or R: No processing between RDRP and helicase. 1 Publication
Mutagenesisi5383 – 53831S → A: No effect. 1 Publication
Mutagenesisi5383 – 53831S → N: No processing between RDRP and helicase. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247Non-structural protein 1 InferredPRO_0000037338Add
BLAST
Chaini248 – 832585Non-structural protein 2 InferredPRO_0000037339Add
BLAST
Chaini833 – 28372005Non-structural protein 3 InferredPRO_0000037340Add
BLAST
Chaini2838 – 3333496Non-structural protein 4PRO_0000037341Add
BLAST
Chaini3334 – 36353023C-like proteinasePRO_0000037342Add
BLAST
Chaini3636 – 3921286Non-structural protein 6 InferredPRO_0000037343Add
BLAST
Chaini3922 – 401392Non-structural protein 7PRO_0000037344Add
BLAST
Chaini4014 – 4207194Non-structural protein 8PRO_0000037345Add
BLAST
Chaini4208 – 4317110Non-structural protein 9PRO_0000037346Add
BLAST
Chaini4318 – 4454137Non-structural protein 10PRO_0000037347Add
BLAST
Chaini4455 – 5382928RNA-directed RNA polymerasePRO_0000037348Add
BLAST
Chaini5383 – 5982600Helicase InferredPRO_0000037349Add
BLAST
Chaini5983 – 6503521Exoribonuclease By similarityPRO_0000037350Add
BLAST
Chaini6504 – 6877374Uridylate-specific endoribonuclease By similarityPRO_0000037351Add
BLAST
Chaini6878 – 7176299Putative 2'-O-methyl transferase By similarityPRO_0000037352Add
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.

Interactioni

Subunit structurei

3CL-PRO exists as monomer and homodimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer By similarity.

Structurei

Secondary structure

1
7176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3246 – 32494
Beta strandi3254 – 32563
Helixi3258 – 326710
Helixi3270 – 32789
Helixi3280 – 32845
Beta strandi3287 – 32904
Helixi3292 – 331322
Beta strandi3318 – 33203
Beta strandi3326 – 33305

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GTHX-ray2.70A6504-6872[»]
2GTIX-ray2.15A6504-6872[»]
3VC8X-ray2.00A/B3245-3333[»]
3VCBX-ray2.40A/B3245-3333[»]
ProteinModelPortaliP0C6X9.
SMRiP0C6X9. Positions 4049-4199, 4323-4447, 6504-6872.

Miscellaneous databases

EvolutionaryTraceiP0C6X9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1084 – 1333250Peptidase C16 1Add
BLAST
Domaini1323 – 1482160MacroAdd
BLAST
Domaini1678 – 1937260Peptidase C16 2Add
BLAST
Domaini3334 – 3635302Peptidase C30Add
BLAST
Domaini5062 – 5224163RdRp catalyticAdd
BLAST
Domaini5383 – 546684CV MBDAdd
BLAST
Domaini5638 – 5819182(+)RNA virus helicase ATP-bindingAdd
BLAST
Domaini5820 – 5989170(+)RNA virus helicase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2225 – 2645421HD1Add
BLAST
Regioni2847 – 3222376HD2Add
BLAST
Regioni3526 – 3860335HD3Add
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.

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. 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: 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.

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MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK     50
GKTLVNHVRV NCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG 100
SAVLVKPSKR LSIQAWTNLG VLPKTAAMGL FKRVCLCNTR ECSCDAHVAF 150
HLFTVQPDGV CLGNGRFIGW FVPVTAIPEY AKQWLQPWSI LLRKGGNKGS 200
VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSCKAYA LLKGYRGVKP 250
ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELFPVWRDS LDSEVLVAWH 300
VDRDPRAAMR LQTLATVRCI DYVGQPTEDV VDGDVVVREP AHLLAANAIV 350
KRLPRLVETM LYTDSSVTEF CYKTKLCECG FITQFGYVDC CGDTCDFRGW 400
VAGNMMDGFP CPGCTKNYMP WELEAQSSGV IPEGGVLFTQ STDTVNRESF 450
KLYGHAVVPF GSAVYWSPCP GMWLPVIWSS VKSYSGLTYT GVVGCKAIVQ 500
ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN RGDYSLLLEN 550
VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN 600
FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT 650
EWFDLAVDIA ASAAGWLCYQ LVNGLFAVAN GVITFVQEVP ELVKNFVDKF 700
KAFFKVLIDS MSVSILSGLT VVKTASNRVC LAGSKVYEVV QKSLSAYVMP 750
VGCSEATCLV GEIEPAVFED DVVDVVKAPL TYQGCCKPPT SFEKICIVDK 800
LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVEFND KPKVRKIPST 850
RKIKITFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC 900
KEHDVIGTKV CALLDRLAGD YVYLFDEGGD EVIAPRMYCS FSAPDDEDCV 950
AADVVDADEN QDDDAEDSAV LVADTQEEDG VAKGQVEADS EICVAHTGSQ 1000
EELAEPDAVG SQTPIASAEE TEVGEASDRE GIAEAKATVC ADAVDACPDQ 1050
VEAFEIEKVE DSILDELQTE LNAPADKTYE DVLAFDAVCS EALSAFYAVP 1100
SDETHFKVCG FYSPAIERTN CWLRSTLIVM QSLPLEFKDL EMQKLWLSYK 1150
AGYDQCFVDK LVKSVPKSII LPQGGYVADF AYFFLSQCSF KAYANWRCLE 1200
CDMELKLQGL DAMFFYGDVV SHMCKCGNSM TLLSADIPYT LHFGVRDDKF 1250
CAFYTPRKVF RAACAVDVND CHSMAVVEGK QIDGKVVTKF IGDKFDFMVG 1300
YGMTFSMSPF ELAQLYGSCI TPNVCFVKGD VIKVVRLVNA EVIVNPANGR 1350
MAHGAGVAGA IAEKAGSAFI KETSDMVKAQ GVCQVGECYE SAGGKLCKKV 1400
LNIVGPDARG HGKQCYSLLE RAYQHINKCD NVVTTLISAG IFSVPTDVSL 1450
TYLLGVVTKN VILVSNNQDD FDVIEKCQVT SVAGTKALSL QLAKNLCRDV 1500
KFVTNACSSL FSESCFVSSY DVLQEVEALR HDIQLDDDAR VFVQANMDCL 1550
PTDWRLVNKF DSVDGVRTIK YFECPGGIFV SSQGKKFGYV QNGSFKEASV 1600
SQIRALLANK VDVLCTVDGV NFRSCCVAEG EVFGKTLGSV FCDGINVTKV 1650
RCSAIYKGKV FFQYSDLSEA DLVAVKDAFG FDEPQLLKYY TMLGMCKWPV 1700
VVCGNYFAFK QSNNNCYINV ACLMLQHLSL KFPKWQWQEA WNEFRSGKPL 1750
RFVSLVLAKG SFKFNEPSDS IDFMRVVLRE ADLSGATCNL EFVCKCGVKQ 1800
EQRKGVDAVM HFGTLDKGDL VRGYNIACTC GSKLVHCTQF NVPFLICSNT 1850
PEGRKLPDDV VAANIFTGGS VGHYTHVKCK PKYQLYDACN VNKVSEAKGN 1900
FTDCLYLKNL KQTFSSVLTT FYLDDVKCVE YKPDLSQYYC ESGKYYTKPI 1950
IKAQFRTFEK VDGVYTNFKL VGHSIAEKLN AKLGFDCNSP FVEYKITEWP 2000
TATGDVVLAS DDLYVSRYSS GCITFGKPVV WLGHEEASLK SLTYFNRPSV 2050
VCENKFNVLP VDVSEPTDKG PVPAAVLVTG VPGADASAGA GIAKEQKACA 2100
SASVEDQVVT EVRQEPSVSA ADVKEVKLNG VKKPVKVEGS VVVNDPTSET 2150
KVVKSLSIVD VYDMFLTGCK YVVWTANELS RLVNSPTVRE YVKWGMGKIV 2200
TPAKLLLLRD EKQEFVAPKV VKAKAIACYC AVKWFLLYCF SWIKFNTDNK 2250
VIYTTEVASK LTFKLCCLAF KNALQTFNWS VVSRGFFLVA TVFLLWFNFL 2300
YANVILSDFY LPNIGPLPTF VGQIVAWFKT TFGVSTICDF YQVTDLGYRS 2350
SFCNGSMVCE LCFSGFDMLD NYDAINVVQH VVDRRLSFDY ISLFKLVVEL 2400
VIGYSLYTVC FYPLFVLIGM QLLTTWLPEF FMLETMHWSA RLFVFVANML 2450
PAFTLLRFYI VVTAMYKVYC LCRHVMYGCS KPGCLFCYKR NRSVRVKCST 2500
VVGGSLRYYD VMANGGTGFC TKHQWNCLNC NSWKPGNTFI THEAAADLSK 2550
ELKRPVNPTD SAYYSVTEVK QVGCSMRLFY ERDGQRVYDD VNASLFVDMN 2600
GLLHSKVKGV PETHVVVVEN EADKAGFLGA AVFYAQSLYR PMLMVEKKLI 2650
TTANTGLSVS RTMFDLYVDS LLNVLDVDRK SLTSFVNAAH NSLKEGVQLE 2700
QVMDTFIGCA RRKCAIDSDV ETKSITKSVM SAVNAGVDFT DESCNNLVPT 2750
YVKSDTIVAA DLGVLIQNNA KHVQANVAKA ANVACIWSVD AFNQLSADLQ 2800
HRLRKACSKT GLKIKLTYNK QEANVPILTT PFSLKGGAVF SRMLQWLFVA 2850
NLICFIVLWA LMPTYAVHKS DMQLPLYASF KVIDNGVLRD VSVTDACFAN 2900
KFNQFDQWYE STFGLAYYRN SKACPVVVAV IDQDIGHTLF NVPTTVLRYG 2950
FHVLHFITHA FATDSVQCYT PHMQIPYDNF YASGCVLSSL CTMLAHADGT 3000
PHPYCYTGGV MHNASLYSSL APHVRYNLAS SNGYIRFPEV VSEGIVRVVR 3050
TRSMTYCRVG LCEEAEEGIC FNFNRSWVLN NPYYRAMPGT FCGRNAFDLI 3100
HQVLGGLVRP IDFFALTASS VAGAILAIIV VLAFYYLIKL KRAFGDYTSV 3150
VVINVIVWCI NFLMLFVFQV YPTLSCLYAC FYFYTTLYFP SEISVVMHLQ 3200
WLVMYGAIMP LWFCIIYVAV VVSNHALWLF SYCRKIGTEV RSDGTFEEMA 3250
LTTFMITKES YCKLKNSVSD VAFNRYLSLY NKYRYFSGKM DTAAYREAAC 3300
SQLAKAMETF NHNNGNDVLY QPPTASVTTS FLQSGIVKMV SPTSKVEPCI 3350
VSVTYGNMTL NGLWLDDKVY CPRHVICSSA DMTDPDYPNL LCRVTSSDFC 3400
VMSGRMSLTV MSYQMQGCQL VLTVTLQNPN TPKYSFGVVK PGETFTVLAA 3450
YNGRPQGAFH VTLRSSHTIK GSFLCGSCGS VGYVLTGDSV RFVYMHQLEL 3500
STGCHTGTDF SGNFYGPYRD AQVVQLPVQD YTQTVNVVAW LYAAIFNRCN 3550
WFVQSDSCSL EEFNVWAMTN GFSSIKADLV LDALASMTGV TVEQVLAAIK 3600
RLHSGFQGKQ ILGSCVLEDE TPSDVYQQLA GVKLQSKRTR VIKGTCCWIL 3650
ASTFLFCSII SAFVKWTMFM YVTTHMLGVT LCALCFVSFA MLLIKHKHLY 3700
LTMYIMPVLC TFYTNYLVVY KQSFRGLAYA WLSHFVPAVD YTYMDEVLYG 3750
VVLLVAMVFV TMRSINHDVF SIMFLVGRLV SLVSMWYFGA NLEEEVLLFL 3800
TSLFGTYTWT TMLSLATAKV IAKWLAVNVL YFTDVPQIKL VLLSYLCIGY 3850
VCCCYWGILS LLNSIFRMPL GVYNYKISVQ ELRYMNANGL RPPRNSFEAL 3900
MLNFKLLGIG GVPVIEVSQI QSRLTDVKCA NVVLLNCLQH LHIASNSKLW 3950
QYCSTLHNEI LATSDLSMAF DKLAQLLVVL FANPAAVDSK CLASIEEVSD 4000
DYVRDNTVLQ ALQSEFVNMA SFVEYELAKK NLDEAKASGS ANQQQIKQLE 4050
KACNIAKSAY ERDRAVARKL ERMADLALTN MYKEARINDK KSKVVSALQT 4100
MLFSMVRKLD NQALNSILDN AVKGCVPLNA IPSLTSNTLT IIVPDKQVFD 4150
QVVDNVYVTY AGNVWHIQFI QDADGAVKQL NEIDVNSTWP LVIAANRHNE 4200
VSTVVLQNNE LMPQKLRTQV VNSGSDMNCN TPTQCYYNTT GTGKIVYAIL 4250
SDCDGLKYTK IVKEDGNCVV LELDPPCKFS VQDVKGLKIK YLYFVKGCNT 4300
LARGWVVGTL SSTVRLQAGT ATEYASNSAI LSLCAFSVDP KKTYLDYIKQ 4350
GGVPVTNCVK MLCDHAGTGM AITIKPEATT NQDSYGGASV CIYCRSRVEH 4400
PDVDGLCKLR GKFVQVPLGI KDPVSYVLTH DVCQVCGFWR DGSCSCVGTG 4450
SQFQSKDTNF LNRIRGTSVN ARLVPCASGL DTDVQLRAFD ICNANRAGIG 4500
LYYKVNCCRF QRVDEDGNKL DKFFVVKRTN LEVYNKEKEC YELTKECGVV 4550
AEHEFFTFDV EGSRVPHIVR KDLSKFTMLD LCYALRHFDR NDCSTLKEIL 4600
LTYAECEESY FQKKDWYDFV ENPDIINVYK KLGPIFNRAL LNTAKFADAL 4650
VEAGLVGVLT LDNQDLYGQW YDFGDFVKTV PGCGVAVADS YYSYMMPMLT 4700
MCHALDSELF VNGTYREFDL VQYDFTDFKL ELFTKYFKHW SMTYHPNTCE 4750
CEDDRCIIHC ANFNILFSMV LPKTCFGPLV RQIFVDGVPF VVSIGYHYKE 4800
LGVVMNMDVD THRYRLSLKD LLLYAADPAL HVASASALLD LRTCCFSVAA 4850
ITSGVKFQTV KPGNFNQDFY EFILSKGLLK EGSSVDLKHF FFTQDGNAAI 4900
TDYNYYKYNL PTMVDIKQLL FVLEVVNKYF EIYEGGCIPA TQVIVNNYDK 4950
SAGYPFNKFG KARLYYEALS FEEQDEIYAY TKRNVLPTLT QMNLKYAISA 5000
KNRARTVAGV SILSTMTGRM FHQKCLKSIA ATRGVPVVIG TTKFYGGWDD 5050
MLRRLIKDVD SPVLMGWDYP KCDRAMPNIL RIVSSLVLAR KHDSCCSHTD 5100
RFYRLANECA QVLSEIVMCG GCYYVKPGGT SSGDATTAFA NSVFNICQAV 5150
SANVCSLMAC NGHKIEDLSI RELQKRLYSN VYRADHVDPA FVSEYYEFLN 5200
KHFSMMILSD DGVVCYNSEF ASKGYIANIS AFQQVLYYQN NVFMSEAKCW 5250
VETDIEKGPH EFCSQHTMLV KMDGDEVYLP YPDPSRILGA GCFVDDLLKT 5300
DSVLLIERFV SLAIDAYPLV YHENPEYQNV FRVYLEYIKK LYNDLGNQIL 5350
DSYSVILSTC DGQKFTDETF YKNMYLRSAV LQSVGACVVC SSQTSLRCGS 5400
CIRKPLLCCK CAYDHVMSTD HKYVLSVSPY VCNSPGCDVN DVTKLYLGGM 5450
SYYCEDHKPQ YSFKLVMNGM VFGLYKQSCT GSPYIEDFNK IASCKWTEVD 5500
DYVLANECTE RLKLFAAETQ KATEEAFKQC YASATIREIV SDRELILSWE 5550
IGKVRPPLNK NYVFTGYHFT NNGKTVLGEY VFDKSELTNG VYYRATTTYK 5600
LSVGDVFILT SHAVSSLSAP TLVPQENYTS IRFASVYSVP ETFQNNVPNY 5650
QHIGMKRYCT VQGPPGTGKS HLAIGLAVYY CTARVVYTAA SHAAVDALCE 5700
KAHKFLNIND CTRIVPAKVR VDCYDKFKVN DTTRKYVFTT INALPELVTD 5750
IIVVDEVSML TNYELSVINS RVRAKHYVYI GDPAQLPAPR VLLNKGTLEP 5800
RYFNSVTKLM CCLGPDIFLG TCYRCPKEIV DTVSALVYNN KLKAKNDNSS 5850
MCFKVYYKGQ TTHESSSAVN MQQIHLISKF LKANPSWSNA VFISPYNSQN 5900
YVAKRVLGLQ TQTVDSAQGS EYDFVIYSQT AETAHSVNVN RFNVAITRAK 5950
KGILCVMSSM QLFESLNFTT LTLDKINNPR LQCTTNLFKD CSRSYVGYHP 6000
AHAPSFLAVD DKYKVGGDLA VCLNVADSAV TYSRLISLMG FKLDLTLDGY 6050
CKLFITRDEA IKRVRAWVGF DAEGAHAIRD SIGTNFPLQL GFSTGIDFVV 6100
EATGMFAERD GYVFKKAAAR APPGEQFKHL IPLMSRGQKW DVVRIRIVQM 6150
LSDHLVDLAD SVVLVTWAAS FELTCLRYFA KVGREVVCSV CTKRATCFNS 6200
RTGYYGCWRH SYSCDYLYNP LIVDIQQWGY TGSLTSNHDP ICSVHKGAHV 6250
ASSDAIMTRC LAVHDCFCKS VNWNLEYPII SNEVSVNTSC RLLQRVMFRA 6300
AMLCNRYDVC YDIGNPKGLA CVKGYDFKFY DASPVVKSVK QFVYKYEAHK 6350
DQFLDGLCMF WNCNVDKYPA NAVVCRFDTR VLNKLNLPGC NGGSLYVNKH 6400
AFHTSPFTRA AFENLKPMPF FYYSDTPCVY MEGMESKQVD YVPLRSATCI 6450
TRCNLGGAVC LKHAEEYREY LESYNTATTA GFTFWVYKTF DFYNLWNTFT 6500
RLQSLENVVY NLVNAGHFDG RAGELPCAVI GEKVIAKIQN EDVVVFKNNT 6550
PFPTNVAVEL FAKRSIRPHP ELKLFRNLNI DVCWSHVLWD YAKDSVFCSS 6600
TYKVCKYTDL QCIESLNVLF DGRDNGALEA FKKCRNGVYI NTTKIKSLSM 6650
IKGPQRADLN GVVVEKVGDS DVEFWFAVRK DGDDVIFSRT GSLEPSHYRS 6700
PQGNPGGNRV GDLSGNEALA RGTIFTQSRL LSSFTPRSEM EKDFMDLDDD 6750
VFIAKYSLQD YAFEHVVYGS FNQKIIGGLH LLIGLARRQQ KSNLVIQEFV 6800
TYDSSIHSYF ITDENSGSSK SVCTVIDLLL DDFVDIVKSL NLKCVSKVVN 6850
VNVDFKDFQF MLWCNEEKVM TFYPRLQAAA DWKPGYVMPV LYKYLESPLE 6900
RVNLWNYGKP ITLPTGCMMN VAKYTQLCQY LSTTTLAVPA NMRVLHLGAG 6950
SDKGVAPGSA VLRQWLPAGS ILVDNDVNPF VSDSVASYYG NCITLPFDCQ 7000
WDLIISDMYD PLTKNIGEYN VSKDGFFTYL CHLIRDKLAL GGSVAIKITE 7050
FSWNAELYSL MGKFAFWTIF CTNVNASSSE GFLIGINWLN KTRTEIDGKT 7100
MHANYLFWRN STMWNGGAYS LFDMSKFPLK AAGTAVVSLK PDQINDLVLS 7150
LIEKGKLLVR DTRKEVFVGD SLVNVK 7176

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 AAB86818.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence AAB86820.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAA36202.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1699 – 16991P → S in strain: Isolate C12 mutant.
Natural varianti2196 – 21961M → K in strain: Isolate C12 mutant.
Natural varianti5773 – 57731R → S in strain: Isolate C12 mutant.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2882WR → CA1 Publication
Sequence conflicti311 – 3111L → V1 Publication
Sequence conflicti570 – 5701D → G1 Publication
Sequence conflicti3620 – 36201E → EL1 Publication
Sequence conflicti3711 – 37111T → TL1 Publication
Sequence conflicti3968 – 39681M → V1 Publication
Sequence conflicti4464 – 44641I → V1 Publication
Sequence conflicti6156 – 61561V → A1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A32440.
S15760.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GTH X-ray 2.70 A 6504-6872 [» ]
2GTI X-ray 2.15 A 6504-6872 [» ]
3VC8 X-ray 2.00 A/B 3245-3333 [» ]
3VCB X-ray 2.40 A/B 3245-3333 [» ]
ProteinModelPortali P0C6X9.
SMRi P0C6X9. Positions 4049-4199, 4323-4447, 6504-6872.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0C6X9.

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. 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 primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism."
    Bredenbeek P.J., Pachuk C.J., Noten A.F.H., Charite J., Luytjes W., Weiss S.R., Spaan W.J.M.
    Nucleic Acids Res. 18:1825-1832(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ORF1B).
  2. "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: NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ORF1A).
  3. "Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is associated with a Q159L amino acid substitution in the spike protein."
    Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.
    Virology 239:1-10(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate C12 mutant.
  4. "Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59."
    Pachuk C.J., Bredenbeek P.J., Zoltick P.W., Spaan W.J.M., Weiss S.R.
    Virology 171:141-148(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-597.
  5. "Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro."
    Lu X.T., Sims A.C., Denison M.R.
    J. Virol. 72:2265-2271(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, CHARACTERIZATION OF NSP8.
  6. "The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis."
    Denison M.R., Spaan W.J.M., van der Meer Y., Gibson C.A., Sims A.C., Prentice E., Lu X.T.
    J. Virol. 73:6862-6871(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION OF HELICASE.
  7. "Further requirements for cleavage by the murine coronavirus 3C-like proteinase: identification of a cleavage site within ORF1b."
    Pinon J.D., Teng H., Weiss S.R.
    Virology 263:471-484(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF PHE-3331; LEU-3332; GLN-3333; SER-3334; GLY-3335; ILE-3336; CYS-3478; LEU-5381; GLN-5382 AND SER-5383.
  8. "Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly."
    Bost A.G., Carnahan R.H., Lu X.T., Denison M.R.
    J. Virol. 74:3379-3387(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, CHARACTERIZATION OF NSP7; NSP9 AND NSP10.

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: September 3, 2014
This is version 53 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

External Data

Dasty 3

Similar proteinsi