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P13899 (POLG_TMEVD) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 13 chains:

  1. Leader protein
  2. Protein VP0
    Alternative name(s):
    VP4-VP2
  3. Protein VP4
    Alternative name(s):
    P1A
    Virion protein 4
  4. Protein VP2
    Alternative name(s):
    P1B
    Virion protein 2
  5. Protein VP3
    Alternative name(s):
    P1C
    Virion protein 3
  6. Protein VP1
    Alternative name(s):
    P1D
    Virion protein 1
  7. Protein 2A
    Short name=P2A
  8. Protein 2B
    Short name=P2B
  9. Protein 2C
    Short name=P2C
    EC=3.6.1.15
  10. Protein 3A
    Short name=P3A
  11. Protein 3B
    Short name=P3B
    Alternative name(s):
    VPg
  12. Protease 3C
    Short name=P3C
    EC=3.4.22.28
    Alternative name(s):
    Picornain 3C
  13. RNA-directed RNA polymerase 3D-POL
    Short name=P3D-POL
    EC=2.7.7.48
OrganismTheiler's murine encephalomyelitis virus (strain DA) (TMEV) [Complete proteome]
Taxonomic identifier12126 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
Virus hostMus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length2301 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Leader protein: promotes host NUP98 phosphorylation and blocks the export of host mRNA from the nucleus. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response. The leader protein also inhibit host interferon regulatory factor 3 (IRF3) dimerization, thereby blocking the transcriptional activation of IFN genes. Ref.3 Ref.4

Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes By similarity. Ref.3 Ref.4

Protein VP0: VP0 precursor is a component of immature procapsids By similarity. Ref.3 Ref.4

Protein 2B: Affects membrane integrity and cause an increase in membrane permeability By similarity. Ref.3 Ref.4

Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity. Ref.3 Ref.4

Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. Ref.3 Ref.4

Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease By similarity. Ref.3 Ref.4

RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. Ref.3 Ref.4

Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function By similarity. Ref.3 Ref.4

Catalytic activity

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.

NTP + H2O = NDP + phosphate.

Subcellular location

Protein 2A: Host nucleus By similarity.

Protein VP2: Virion. Host cytoplasm Potential.

Protein VP3: Virion. Host cytoplasm Potential.

Protein VP1: Virion. Host cytoplasm Potential.

Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.

Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.

Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.

Protein 3B: Virion Potential.

Protease 3C: Host cytoplasm Potential.

RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.

Domain

The Theilo and zinc-finger regions may both play a role in the inhibition of host mRNA export and IRF-3 dimerization antagonism by the L protein.

Post-translational modification

Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex By similarity.

VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.

Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.

Miscellaneous

Persistent strains of Theiler's virus (e.g. DA, TO, BeAn) cause persistent demyelinating disease whereas neurovirulent strains (such as GDVII) cause acute encephalitis.

Sequence similarities

Belongs to the picornaviruses polyprotein family.

Contains 2 peptidase C3 domains.

Contains 1 RdRp catalytic domain.

Contains 1 SF3 helicase domain.

Ontologies

Keywords
   Biological processEukaryotic host gene expression shutoff by virus
Eukaryotic host translation shutoff by virus
Host gene expression shutoff by virus
Host-virus interaction
Inhibition of host innate immune response by virus
Inhibition of host IRF3 by virus
Inhibition of host RLR pathway by virus
Ion transport
Transport
Viral attachment to host cell
Viral immunoevasion
Viral RNA replication
Virus entry into host cell
   Cellular componentCapsid protein
Host cytoplasm
Host cytoplasmic vesicle
Host membrane
Host nucleus
Membrane
Virion
   DomainZinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
   Molecular functionHelicase
Hydrolase
Ion channel
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Thiol protease
Transferase
Viral ion channel
   PTMCovalent protein-RNA linkage
Lipoprotein
Myristate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processRNA-protein covalent cross-linking

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

pore formation by virus in membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

protein oligomerization

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host IRF3 activity

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host RIG-I activity by RIG-I proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

suppression by virus of host mRNA export from nucleus

Inferred from direct assay Ref.3. Source: UniProtKB

suppression by virus of host translation

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: InterPro

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

icosahedral viral capsid

Inferred from electronic annotation. Source: InterPro

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676Leader protein
PRO_0000040180
Chain77 – 414338Protein VP0 Potential
PRO_0000310971
Chain77 – 14771Protein VP4 Potential
PRO_0000040181
Chain148 – 414267Protein VP2 Potential
PRO_0000040182
Chain415 – 646232Protein VP3 Potential
PRO_0000040183
Chain647 – 920274Protein VP1 Potential
PRO_0000040184
Chain921 – 1053133Protein 2A Potential
PRO_0000040185
Chain1054 – 1189136Protein 2B Potential
PRO_0000040186
Chain1190 – 1515326Protein 2C Potential
PRO_0000040187
Chain1516 – 160388Protein 3A Potential
PRO_0000040188
Chain1604 – 162320Protein 3B Potential
PRO_0000040189
Chain1624 – 1840217Protease 3C Potential
PRO_0000040190
Chain1841 – 2301461RNA-directed RNA polymerase 3D-POL Potential
PRO_0000040191

Regions

Topological domain1 – 15601560Cytoplasmic Potential
Intramembrane1561 – 157919 Potential
Topological domain1580 – 2301722Cytoplasmic Potential
Domain1281 – 1446166SF3 helicase
Domain2069 – 2187119RdRp catalytic
Zinc finger3 – 1412 Potential
Nucleotide binding1310 – 13178ATP Potential
Region30 – 4617Acidic
Region60 – 7314Theilo

Sites

Active site16781For protease 3C activity Potential
Active site17101For protease 3C activity Potential
Active site17911For protease 3C activity Potential
Site147 – 1482Cleavage Potential
Site414 – 4152Cleavage; by protease 3C Potential
Site646 – 6472Cleavage; by protease 3C Potential
Site920 – 9212Cleavage; by protease 3C Potential
Site1053 – 10542Cleavage; by ribosomal skip Potential
Site1189 – 11902Cleavage; by protease 3C Potential
Site1515 – 15162Cleavage; by protease 3C Potential
Site1603 – 16042Cleavage; by protease 3C Potential
Site1623 – 16242Cleavage; by protease 3C Potential
Site1840 – 18412Cleavage; by protease 3C Potential

Amino acid modifications

Modified residue16061O-(5'-phospho-RNA)-tyrosine By similarity
Lipidation771N-myristoyl glycine; by host By similarity

Secondary structure

......................................................................................................................... 2301
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13899 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 0B6095DF153DBFDF

FASTA2,301256,161
        10         20         30         40         50         60 
MACKHGYPDV CPICTAVDVT PGFEYLLLAD GEWFPTDLLC VDLDDDVFWP SNSSNQSETM 

        70         80         90        100        110        120 
EWTDLPLVRD IVMEPQGNAS SSDKSNSQSS GNEGVIINNF YSNQYQNSID LSASGGNAGD 

       130        140        150        160        170        180 
APQNNGQLSN ILGGAANAFA TMAPLLLDQN TEEMENLSDR VASDKAGNSA TNTQSTVGRL 

       190        200        210        220        230        240 
CGYGEAHHGE HPASCADTAT DKVLAAERYY TIDLASWTTT QEAFSHIRIP LPHVLAGEDG 

       250        260        270        280        290        300 
GVFGATLRRH YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG DMEPTDPFTM 

       310        320        330        340        350        360 
DTTWRAPQGA PTGYRYDSRT GFFAMNHQNQ WQWTVYPHQI LNLRTNTTVD LEVPYVNIAP 

       370        380        390        400        410        420 
TSSWTQHANW TLVVAVFSPL QYASGSSSDV QITASIQPVN PVFNGLRHET VIAQSPIAVT 

       430        440        450        460        470        480 
VREHKGCFYS TNPDTTVPIY GKTISTPNDY MCGEFSDLLE LCKLPTFLGN PNSNNKRYPY 

       490        500        510        520        530        540 
FSATNSVPTT SLVDYQVALS CSCMCNSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL 

       550        560        570        580        590        600 
IAYTPPGAGK PTTRDQAMQA TYAIWDLGLN SSFVFTAPFI SPTHYRQTSY TSATIASVDG 

       610        620        630        640        650        660 
WVTVWQLTPL TYPSGAPVNS DILTLVSAGD DFTLRMPISP TKWAPQGSDN AEKGKVSNDD 

       670        680        690        700        710        720 
ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNIES TFVYQENDLR LNCLLLTPLP 

       730        740        750        760        770        780 
SFCPDSTSGP VKTKAPVQWR WVRSGGTTNF PLMTKQDYAF LCFSPFTYYK CDLEVTVSAL 

       790        800        810        820        830        840 
GTDTVASVLR WAPTGAPADV TDQLIGYTPS LGETRNPHMW LVGAGNTQIS FVVPYNSPLS 

       850        860        870        880        890        900 
VLPAAWFNGW SDFGNTKDFG VAPNADFGRL WIQGNTSASV RIRYKKMKVF CPRPTLFFPW 

       910        920        930        940        950        960 
PVSTRSKINA DNPVPILELE NPAAFYRIDL FITFIDEFIT FDYKVHGRPV LTFRIPGFGL 

       970        980        990       1000       1010       1020 
TPAGRMLVCM GEKPAHGPFT SSRSLYHVIF TATCSSFSFS IYKGRYRSWK KPIHDELVDR 

      1030       1040       1050       1060       1070       1080 
GYTTFGEFFR AVRAYHADYY KQRLIHDVEM NPGPVQSVFQ PQGAVLTKSL APQAGIQNLL 

      1090       1100       1110       1120       1130       1140 
LRLLGIDGDC SEVSKAITVV TDLFAAWERA KTTLVSPEFW SKLILKTTKF IAASVLYLHN 

      1150       1160       1170       1180       1190       1200 
PDFTTTVCLS LMTGVDLLTN DSVFDWLKNK LSSFFRTPPP VCPNVLQPQG PLREANEGFT 

      1210       1220       1230       1240       1250       1260 
FAKNIEWAMK TIQSIVNWLT SWFKQEEDHP QSKLDKFLME FPDHCRNIMD MRNGRKAYCE 

      1270       1280       1290       1300       1310       1320 
CTASFKYFDE LYNLAVTCKR IPLASLCEKF KNRHDHSVTR PEPVVVVLRG AAGQGKSVTS 

      1330       1340       1350       1360       1370       1380 
QIIAQSVSKM AFGRQSVYSM PPDSEYFDGY ENQFSVIMDD LGQNPDGEDF TVFCQMVSST 

      1390       1400       1410       1420       1430       1440 
NFLPNMAHLE RKGTPFTSSF IVATTNLPKF RPVTVAHYPA VDRRITFDFT VTAGPHCTTS 

      1450       1460       1470       1480       1490       1500 
NGMLDIEKAF DEIPGSKPQL ACFSADCPLL HKRGVMFTCN RTKAVYNLQQ VVKMVNDTIT 

      1510       1520       1530       1540       1550       1560 
RKTENVKKMN SLVAQSPPDW EHFENILTCL RQNNAALQDQ LDELQEAFAQ ARERSDFLSD 

      1570       1580       1590       1600       1610       1620 
WLKVSAIIFA GIASLSAVIK LASKFKESIW PSPVRVELSE GEQAAYAGRA RAQKQALQVL 

      1630       1640       1650       1660       1670       1680 
DIQGGGKVLA QAGNPVMDFE LFCAKNMVAP ITFYYPDKAE VTQSCLLLRA HLFVVNRHVA 

      1690       1700       1710       1720       1730       1740 
ETEWTAFKLK DVRHERDTVV TRSVNRSGAE TDLTFIKVTK GPLFKDNVNK FCSNKDDFPA 

      1750       1760       1770       1780       1790       1800 
RNDAVTGIMN TGLAFVYSGN FLIGNQPVNT TTGACFNHCL HYRAQTRRGW CGSAVICNVN 

      1810       1820       1830       1840       1850       1860 
GKKAVYGMHS AGGGGLAAAT IITRELIEAA EKSMLALEPQ GAIVDISTGS VVHVPRKTKL 

      1870       1880       1890       1900       1910       1920 
RRTVAHDVFQ PKFEPAVLSR YDPRTDKDVD VVAFSKHTTN MESLPPVFDI VCDEYANRVF 

      1930       1940       1950       1960       1970       1980 
TILGKDNGLL TVEQAVLGLP GMDPMEKDTS PGLPYTQQGL RRTDLLNFNT AKMTPQLDYA 

      1990       2000       2010       2020       2030       2040 
HSKLVLGVYD DVVYQSFLKD EIRPLEKIHE AKTRIVDVPP FAHCIWGRQL LGRFASKFQT 

      2050       2060       2070       2080       2090       2100 
KPGLELGSAI GTDPDVDWTP YAAELSGFNY VYDVDYSNFD ASHSTAMFEC LIKNFFTEQN 

      2110       2120       2130       2140       2150       2160 
GFDRRIAEYL RSLAVSRHAY EDRRVLIRGG LLSGCAATSM LNTIMNNVII RAALYLTYSN 

      2170       2180       2190       2200       2210       2220 
FEFDDIKVLS YGDDLLIGTN YQIDFNLVKE RLAPFGYKIT PANKTTTFPL TSHLQDVTFL 

      2230       2240       2250       2260       2270       2280 
KRRFVRFNSY LFRPQMDAVN LKAMVSYCKP GTLKEKLMSI ALLAVHSGPD IYDEIFLPFR 

      2290       2300 
NVGIVVPTYS SMLYRWLSLF R 

« Hide

References

[1]"Molecular cloning and sequence determination of DA strain of Theiler's murine encephalomyelitis viruses."
Ohara Y., Stein S., Fu J., Stillman L., Klaman L., Roos R.P.
Virology 164:245-255(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Alternative translation initiation site in the DA strain of Theiler's murine encephalomyelitis virus."
Kong W.P., Roos R.P.
J. Virol. 65:3395-3399(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION.
[3]"Inhibition of mRNA export and dimerization of interferon regulatory factor 3 by Theiler's virus leader protein."
Ricour C., Delhaye S., Hato S.V., Olenyik T.D., Michel B., van Kuppeveld F.J., Gustin K.E., Michiels T.
J. Gen. Virol. 90:177-186(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE LEADER PROTEIN.
[4]"Random mutagenesis defines a domain of Theiler's virus leader protein that is essential for antagonism of nucleocytoplasmic trafficking and cytokine gene expression."
Ricour C., Borghese F., Sorgeloos F., Hato S.V., van Kuppeveld F.J., Michiels T.
J. Virol. 83:11223-11232(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE LEADER PROTEIN.
[5]"Three-dimensional structure of Theiler virus."
Grant R.A., Filman D.J., Fujinami R.S., Icenogle J.P., Hogle J.M.
Proc. Natl. Acad. Sci. U.S.A. 89:2061-2065(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20301 Genomic RNA. Translation: AAA47928.1.
PIRGNNYTN. A31228.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TMEX-ray2.801647-920[»]
2148-414[»]
3415-650[»]
477-147[»]
1TMFX-ray3.50490-130[»]
ProteinModelPortalP13899.
SMRP13899. Positions 85-146, 159-413, 415-902.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProIPR015031. Capsid_VP4_Picornavir.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamPF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
[Graphical view]
PRINTSPR00918. CALICVIRUSNS.
ProDomPD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13899.

Entry information

Entry namePOLG_TMEVD
AccessionPrimary (citable) accession number: P13899
Secondary accession number(s): Q88564 expand/collapse secondary AC list , Q88565, Q88566, Q88567, Q88568, Q88569, Q88570, Q88571, Q88572, Q88573, Q88574, Q89580
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references