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P14350 (POL_FOAMV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pro-Pol polyprotein
Alternative name(s):
Pr125Pol

Cleaved into the following 4 chains:

  1. Protease/Reverse transcriptase/ribonuclease H
    EC=2.7.7.49
    EC=2.7.7.7
    EC=3.1.26.4
    EC=3.4.23.-
    Alternative name(s):
    p87Pro-RT-RNaseH
  2. Protease/Reverse transcriptase
    EC=2.7.7.49
    EC=2.7.7.7
    EC=3.4.23.-
    Alternative name(s):
    p65Pro-RT
  3. Ribonuclease H
    Short name=RNase H
    EC=3.1.26.4
  4. Integrase
    Short name=IN
    Alternative name(s):
    p42In
Gene names
Name:pol
OrganismHuman spumaretrovirus (SFVcpz(hu)) (Human foamy virus) [Complete proteome]
Taxonomic identifier11963 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeSpumaretrovirinaeSpumavirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1143 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The aspartyl protease activity mediates proteolytic cleavages of Gag and Pol polyproteins. The reverse transcriptase (RT) activity converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell (early reverse transcription) or after proviral DNA transcription (late reverse transcription). RT consists of a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA-Lys1,2 binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primer. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends By similarity.

Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising at least the viral genome, matrix protein, and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from the 3' end of the viral DNA right (U5) end, leaving the left (U3) intact. In the second step, the PIC enters cell nucleus. This process is mediated through the integrase and allows the virus to infect both dividing (nuclear membrane disassembled) and G1/S-arrested cells (active translocation), but with no viral gene expression in the latter. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. It is however not clear how integration then proceeds to resolve the asymmetrical cleavage of viral DNA By similarity.

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester.

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Cofactor

Binds 2 magnesium ions for reverse transcriptase polymerase activity By similarity.

Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding By similarity.

Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.

Subunit structure

The protease is a homodimer, whose active site consists of two apposed aspartic acid residues By similarity.

Subcellular location

Integrase: Virion Potential. Host nucleus. Host cytoplasm Potential. Note: Nuclear at initial phase, cytoplasmic at assembly Potential. Ref.9

Protease/Reverse transcriptase/ribonuclease H: Host nucleus By similarity. Host cytoplasm Potential. Note: Nuclear at initial phase, cytoplasmic at assembly Potential. Ref.9

Domain

The reverse transcriptase/ribonuclease H (RT) is structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the "primer grip" region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RNase H domain stabilizes the association of RT with primer-template By similarity.

Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D35E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein By similarity.

Post-translational modification

Specific enzymatic cleavages in vivo by viral protease yield mature proteins. The protease is not cleaved off from Pol. Since cleavage efficiency is not optimal for all sites, long and active p65Pro-RT, p87Pro-RT-RNaseH and even some Pr125Pol are detected in infected cells. Ref.8

Miscellaneous

The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.

Foamy viruses are distinct from other retroviruses in many respects. Their protease is active as an uncleaved Pro-Pol protein. Mature particles do not include the usual processed retroviral structural protein (MA, CA and NC), but instead contain two large Gag proteins. Their functional nucleic acid appears to be either RNA or dsDNA (up to 20% of extracellular particles), because they probably proceed either to an early (before integration) or late reverse transcription (after assembly). Foamy viruses have the ability to retrotranspose intracellularly with high efficiency. They bud predominantly into the endoplasmic reticulum (ER) and occasionally at the plasma membrane. Budding requires the presence of Env proteins. Most viral particles probably remain within the infected cell.

Sequence similarities

Contains 1 integrase catalytic domain.

Contains 1 peptidase A9 domain.

Contains 1 reverse transcriptase domain.

Contains 1 RNase H domain.

Sequence caution

The sequence AAA46122.1 differs from that shown. Reason: Frameshift at position 1075.

The sequence AAA66556.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDNA integration
DNA recombination
Viral genome integration
Viral penetration into host nucleus
Virus entry into host cell
   Cellular componentHost cytoplasm
Host nucleus
Virion
   LigandMagnesium
Metal-binding
RNA-binding
   Molecular functionAspartyl protease
DNA-directed DNA polymerase
Endonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Protease
RNA-directed DNA polymerase
Transferase
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

establishment of integrated proviral latency

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

viral entry into host cell

Inferred from electronic annotation. Source: UniProtKB-KW

viral penetration into host nucleus

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular

Inferred from electronic annotation. Source: GOC

virion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-DNA hybrid ribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

RNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

aspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11431143Pro-Pol polyprotein
PRO_0000125483
Chain1 – 751751Protease/Reverse transcriptase/ribonuclease H
PRO_0000245443
Chain1 – 596596Protease/Reverse transcriptase
PRO_0000245444
Chain597 – 751155Ribonuclease H
PRO_0000245445
Chain752 – 1143392Integrase
PRO_0000245446

Regions

Domain1 – 143143Peptidase A9
Domain198 – 363166Reverse transcriptase
Domain590 – 748159RNase H
Domain868 – 1024157Integrase catalytic

Sites

Active site241For protease activity Probable
Metal binding2521Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding3141Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding3151Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding5991Magnesium; catalytic; for RNase H activity Probable
Metal binding6461Magnesium; catalytic; for RNase H activity By similarity
Metal binding6691Magnesium; catalytic; for RNase H activity By similarity
Metal binding7401Magnesium; catalytic; for RNase H activity By similarity
Metal binding8741Magnesium; catalytic; for integrase activity By similarity
Metal binding9361Magnesium; catalytic; for integrase activity By similarity
Site596 – 5972Cleavage; by viral protease; partial
Site751 – 7522Cleavage; by viral protease

Experimental info

Mutagenesis241D → A: Complete loss of Gag processing and of Pol processing. Particles are non-infectious. Ref.5
Mutagenesis251S → T: No effect on polyprotein processing and viral replication. Ref.5
Mutagenesis1521P → G: No effect on RT or RNase H activities. Ref.6
Mutagenesis1691P → G: 30% loss of RT activity. Ref.6
Mutagenesis1931P → G: 40% loss of RT activity. Ref.6
Mutagenesis5991D → A: 95% loss of RNase H activity. Ref.6
Mutagenesis6721Y → F: 50% loss of RNase H activity. Ref.6

Secondary structure

....................................................................................................... 1143
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14350 [UniParc].

Last modified July 11, 2006. Version 2.
Checksum: 786E3203B06FFB3C

FASTA1,143129,742
        10         20         30         40         50         60 
MNPLQLLQPL PAEIKGTKLL AHWDSGATIT CIPESFLEDE QPIKKTLIKT IHGEKQQNVY 

        70         80         90        100        110        120 
YVTFKVKGRK VEAEVIASPY EYILLSPTDV PWLTQQPLQL TILVPLQEYQ EKILSKTALP 

       130        140        150        160        170        180 
EDQKQQLKTL FVKYDNLWQH WENQVGHRKI RPHNIATGDY PPRPQKQYPI NPKAKPSIQI 

       190        200        210        220        230        240 
VIDDLLKQGV LTPQNSTMNT PVYPVPKPDG RWRMVLDYRE VNKTIPLTAA QNQHSAGILA 

       250        260        270        280        290        300 
TIVRQKYKTT LDLANGFWAH PITPESYWLT AFTWQGKQYC WTRLPQGFLN SPALFTADVV 

       310        320        330        340        350        360 
DLLKEIPNVQ VYVDDIYLSH DDPKEHVQQL EKVFQILLQA GYVVSLKKSE IGQKTVEFLG 

       370        380        390        400        410        420 
FNITKEGRGL TDTFKTKLLN ITPPKDLKQL QSILGLLNFA RNFIPNFAEL VQPLYNLIAS 

       430        440        450        460        470        480 
AKGKYIEWSE ENTKQLNMVI EALNTASNLE ERLPEQRLVI KVNTSPSAGY VRYYNETGKK 

       490        500        510        520        530        540 
PIMYLNYVFS KAELKFSMLE KLLTTMHKAL IKAMDLAMGQ EILVYSPIVS MTKIQKTPLP 

       550        560        570        580        590        600 
ERKALPIRWI TWMTYLEDPR IQFHYDKTLP ELKHIPDVYT SSQSPVKHPS QYEGVFYTDG 

       610        620        630        640        650        660 
SAIKSPDPTK SNNAGMGIVH ATYKPEYQVL NQWSIPLGNH TAQMAEIAAV EFACKKALKI 

       670        680        690        700        710        720 
PGPVLVITDS FYVAESANKE LPYWKSNGFV NNKKKPLKHI SKWKSIAECL SMKPDITIQH 

       730        740        750        760        770        780 
EKGISLQIPV FILKGNALAD KLATQGSYVV NCNTKKPNLD AELDQLLQGH YIKGYPKQYT 

       790        800        810        820        830        840 
YFLEDGKVKV SRPEGVKIIP PQSDRQKIVL QAHNLAHTGR EATLLKIANL YWWPNMRKDV 

       850        860        870        880        890        900 
VKQLGRCQQC LITNASNKAS GPILRPDRPQ KPFDKFFIDY IGPLPPSQGY LYVLVVVDGM 

       910        920        930        940        950        960 
TGFTWLYPTK APSTSATVKS LNVLTSIAIP KVIHSDQGAA FTSSTFAEWA KERGIHLEFS 

       970        980        990       1000       1010       1020 
TPYHPQSGSK VERKNSDIKR LLTKLLVGRP TKWYDLLPVV QLALNNTYSP VLKYTPHQLL 

      1030       1040       1050       1060       1070       1080 
FGIDSNTPFA NQDTLDLTRE EELSLLQEIR TSLYHPSTPP ASSRSWSPVV GQLVQERVAR 

      1090       1100       1110       1120       1130       1140 
PASLRPRWHK PSTVLKVLNP RTVVILDHLG NNRTVSIDNL KPTSHQNGTT NDTATMDHLE 


KNE 

« Hide

References

[1]Fluegel R.M.
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], SEQUENCE REVISION.
[2]"Long terminal repeat U3-length polymorphism of human foamy virus."
Schmidt M., Herchenrder O., Heeney J.L., Rethwilm A.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of the primary structure of the long terminal repeat and the gag and pol genes of the human spumaretrovirus."
Maurer B., Bannert H., Darai G., Fluegel R.M.
J. Virol. 62:1590-1597(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-742.
[4]"Nucleotide sequence analysis of the env gene and its flanking regions of the human spumaretrovirus reveals two novel genes."
Fluegel R.M., Rethwilm A., Maurer B., Darai G.
EMBO J. 6:2077-2084(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 741-886.
[5]"Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein."
Konvalinka J., Loechelt M., Zentgraf H., Fluegel R.M., Kraeusslich H.-G.
J. Virol. 69:7264-7268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE OF PROTEASE, MUTAGENESIS OF ASP-24 AND SER-25.
[6]"Mutational analysis of the reverse transcriptase and ribonuclease H domains of the human foamy virus."
Kogel D., Aboud M., Fluegel R.M.
Nucleic Acids Res. 23:2621-2625(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-152; PRO-169; PRO-193; ASP-599 AND TYR-672.
[7]"The human foamy virus pol gene is expressed as a Pro-Pol polyprotein and not as a Gag-Pol fusion protein."
Loechelt M., Fluegel R.M.
J. Virol. 70:1033-1040(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF POLYPROTEIN.
[8]"Molecular characterization of proteolytic processing of the Pol proteins of human foamy virus reveals novel features of the viral protease."
Pfrepper K.-I., Rackwitz H.R., Schnoelzer M., Heid H., Loechelt M., Fluegel R.M.
J. Virol. 72:7648-7652(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[9]"Primate foamy virus Pol proteins are imported into the nucleus."
Imrich H., Heinkelein M., Herchenroder O., Rethwilm A.
J. Gen. Virol. 81:2941-2947(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: Isolate HSRV2.
[10]"Biphasic DNA synthesis in spumaviruses."
Delelis O., Saib A., Sonigo P.
J. Virol. 77:8141-8146(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF REVERSE TRANSCRIPTASE.
[11]"Foamy virus integration."
Juretzek T., Holm T., Gartner K., Kanzler S., Lindemann D., Herchenroder O., Picard-Maureau M., Rammling M., Heinkelein M., Rethwilm A.
J. Virol. 78:2472-2477(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF INTEGRASE.
[12]"Proteolytic processing of foamy virus Gag and Pol proteins."
Fluegel R.M., Pfrepper K.-I.
Curr. Top. Microbiol. Immunol. 277:63-88(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Foamy viruses-a world apart."
Delelis O., Lehmann-Che J., Saib A.
Curr. Opin. Microbiol. 7:400-406(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U21247 Genomic RNA. Translation: AAB48112.1.
Y07723 Genomic DNA. Translation: CAA68997.1.
Y07724 Genomic DNA. Translation: CAA68999.1.
Y07725 Genomic DNA. Translation: CAA69003.1.
M19427 Genomic RNA. Translation: AAA66556.1. Different initiation.
M54978 Genomic RNA. Translation: AAA46122.1. Frameshift.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LSNNMR-A591-751[»]
2X6NX-ray2.06A/B/C/D/E/F861-1060[»]
2X6SX-ray2.29A/B/C/D/E/F861-1060[»]
2X74X-ray2.34A/B/C/D/E/F861-1060[»]
2X78X-ray2.00A/B/C861-1060[»]
3DLRX-ray2.20A860-1058[»]
3L2QX-ray3.25A/B752-1143[»]
3L2RX-ray2.88A/B752-1143[»]
3L2UX-ray3.15A/B752-1143[»]
3L2VX-ray3.20A/B752-1143[»]
3L2WX-ray3.20A/B752-1143[»]
3OS0X-ray2.81A/B752-1143[»]
3OS1X-ray2.97A/B752-1143[»]
3OS2X-ray3.32A/B752-1143[»]
3OY9X-ray2.95A/B752-1143[»]
3OYAX-ray2.85A/B752-1143[»]
3OYBX-ray2.54A/B752-1143[»]
3OYCX-ray2.66A/B752-1143[»]
3OYDX-ray2.54A/B752-1143[»]
3OYEX-ray2.74A/B752-1143[»]
3OYFX-ray2.51A/B752-1143[»]
3OYGX-ray2.56A/B752-1143[»]
3OYHX-ray2.74A/B752-1143[»]
3OYIX-ray2.72A/B752-1143[»]
3OYJX-ray2.68A/B752-1143[»]
3OYKX-ray2.72A/B752-1143[»]
3OYLX-ray2.54A/B752-1143[»]
3OYMX-ray2.02A/B752-1143[»]
3OYNX-ray2.68A/B752-1143[»]
3S3MX-ray2.49A/B752-1143[»]
3S3NX-ray2.49A/B752-1143[»]
3S3OX-ray2.55A/B752-1143[»]
4BACX-ray3.26A/B752-1143[»]
4BDYX-ray2.52A/B752-1143[»]
4BDZX-ray2.85A/B752-1143[»]
4BE0X-ray2.68A/B752-1143[»]
4BE1X-ray2.71A/B752-1143[»]
4BE2X-ray2.38A/B752-1143[»]
4E7HX-ray2.57A/B752-1143[»]
4E7IX-ray2.53A/B752-1143[»]
4E7JX-ray3.15A/B752-1143[»]
4E7KX-ray3.02A/B752-1143[»]
4E7LX-ray3.00A/B752-1143[»]
4IKFX-ray3.40A/B752-1143[»]
ProteinModelPortalP14350.
SMRP14350. Positions 8-98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-58582N.

Protein family/group databases

MEROPSA09.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.420.10. 2 hits.
InterProIPR001584. Integrase_cat-core.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR001641. Spumavirus_A9.
[Graphical view]
PfamPF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00078. RVT_1. 1 hit.
PF03539. Spuma_A9PTase. 1 hit.
[Graphical view]
PRINTSPR00920. SPUMVIRPTASE.
ProDomPD013079. Peptidase_A9_cat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF53098. SSF53098. 2 hits.
PROSITEPS51531. FV_PR. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14350.
PMAP-CutDBO12817.

Entry information

Entry namePOL_FOAMV
AccessionPrimary (citable) accession number: P14350
Secondary accession number(s): O12528 expand/collapse secondary AC list , O12817, Q76U32, Q98835
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 11, 2006
Last modified: April 16, 2014
This is version 118 of the entry and version 2 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