Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23427 (POL_VILV2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Pol polyprotein

Cleaved into the following 4 chains:

  1. Protease
    Alternative name(s):
    Retropepsin
    EC=3.4.23.-
  2. Reverse transcriptase/ribonuclease H
    Short name=RT
    EC=2.7.7.49
    EC=3.1.26.13
    Alternative name(s):
    Exoribonuclease H
    EC=3.1.13.2
  3. Deoxyuridine 5'-triphosphate nucleotidohydrolase
    Short name=dUTPase
    EC=3.6.1.23
  4. Integrase
    Short name=IN
Gene names
Name:pol
OrganismMaedi visna virus (strain 1514 / clone LV1-1KS2) (MVV) (Visna lentivirus)
Taxonomic identifier11744 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusOvine/caprine lentivirus group
Virus hostOvis aries (Sheep) [TaxID: 9940]

Protein attributes

Sequence length1105 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase.

Catalytic activity

Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.

3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.

dUTP + H2O = dUMP + diphosphate.

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

Post-translational modification

Cleavage sites that yield the mature proteins remain to be determined.

Miscellaneous

This protein may be synthesized as a Gag-Pol polyprotein.

Sequence similarities

Belongs to the retroviral Pol polyprotein family.

Contains 1 integrase catalytic domain.

Contains 1 integrase-type DNA-binding domain.

Contains 1 integrase-type zinc finger.

Contains 1 peptidase A2 domain.

Contains 1 reverse transcriptase domain.

Contains 1 RNase H domain.

Ontologies

Keywords
   Biological processDNA integration
DNA recombination
Nucleotide metabolism
Viral genome integration
Virus entry into host cell
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionAspartyl protease
Endonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Protease
RNA-directed DNA polymerase
Transferase
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Biological_processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

dUTP metabolic process

Inferred from electronic annotation. Source: InterPro

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

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: InterPro

RNA-DNA hybrid ribonuclease activity

Inferred from electronic annotation. Source: InterPro

RNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

aspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

dUTP diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

exoribonuclease H activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 139139Protease By similarity
PRO_0000038865
Chain140 – 690551Reverse transcriptase/ribonuclease H By similarity
PRO_0000038866
Chain691 – 824134Deoxyuridine 5'-triphosphate nucleotidohydrolase By similarity
PRO_0000038867
Chain825 – 1105281Integrase By similarity
PRO_0000038868

Regions

Domain58 – 12972Peptidase A2
Domain186 – 375190Reverse transcriptase
Domain570 – 692123RNase H
Domain869 – 1029161Integrase catalytic
Zinc finger827 – 86842Integrase-type
DNA binding1046 – 109853Integrase-type

Sites

Active site631 By similarity

Sequences

Sequence LengthMass (Da)Tools
P23427 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 34F9E772E96DB520

FASTA1,105126,623
        10         20         30         40         50         60 
TRNNMPSLWK KRTYAKGLPA EETAGKQQEG ATCGAVRAPY VVTEAPPKIE IKVGTRWKKL 

        70         80         90        100        110        120 
LVDTGADKTI VTSHDMSGIP KGRIILQGIG GIIEGEKWEQ VHLQYKDKMI KGTIVVLATS 

       130        140        150        160        170        180 
PVEVLGRDNM RELGIGLIMA NLEEKKIPST RVRLKEGCKG PHIAQWPLTQ EKLEGLKEIV 

       190        200        210        220        230        240 
DRLEKEGKVG RAPPHWTCNT PIFCIKKKSG KWRMLIDFRE LNKQTEDLAE AQLGLPHPGG 

       250        260        270        280        290        300 
LQRKKHVTIL DIGDAYFTIP LYEPYRQYTC FTMLSPNNLG PCVRYYWKVL PQGWKLSPAV 

       310        320        330        340        350        360 
YQFTMQKILR GWIEEHPMIQ FGIYMDDIYI GSDLGLEEHR GIVNELASYI AQYGFMLPED 

       370        380        390        400        410        420 
KRQEGYPAKW LGFELHPEKW KFQKHTLPEI TEGPITLNKL QKLVGDLVWR QSLIGKSIPN 

       430        440        450        460        470        480 
ILKLMEGDRA LQSERYIESI HVREWEACRQ KLKEMEGNYY DEEKDIYGQL DWGNKAIEYI 

       490        500        510        520        530        540 
VFQEKGKPLW VNVVHSIKNL SQAQQIIKAA QKLTQEVIIR TGKIPWILLP GREEDWILEL 

       550        560        570        580        590        600 
QMGNINWMPS FWSCYKGSVR WKKRNVIAEV VPGPTYYTDG GKKNGRGSLG YIASTGEKFR 

       610        620        630        640        650        660 
IHEEGTNQQL ELRAIEEACK QGPEKMNIVT DSRYAYEFML RNWDEEVIRN PIQARIMELV 

       670        680        690        700        710        720 
HNKEKIGVHW VPGHKGIPQN EEIDRYISEI FLAKEGRGIL QKRAEDAGYD LICPQEISIP 

       730        740        750        760        770        780 
AGQVKRIAID LKINLKKDQW AMIGTKSSFA NKGVFVQGGI IDSGYQGTIQ VVIYNSNNKE 

       790        800        810        820        830        840 
VVIPQGRKFA QLILMPLIHE ELKPWGETRK TERGEQGFGS TGMYWIENIP LAEEEHNKWH 

       850        860        870        880        890        900 
QDAVSLHLEF GIPRTAAEDI VQQCDVCQEN KMPSTLRGSN KRGIDHWQVD YTHYEDKIIL 

       910        920        930        940        950        960 
VWVETNSGLI YAERVKGETG QEFRVQTMKW YAMFAPKSLQ SDNGPAFVAE STQLLMKYLG 

       970        980        990       1000       1010       1020 
IEHTTGIPWN PQSQALVERT HQTLKNTLEK LIPMFNAFES ALAGTLITLN IKRKGGLGTS 

      1030       1040       1050       1060       1070       1080 
PMDIFIFNKE QQRIQQQSKS KQEKIRFCYY RTRKRGHPGE WQGPTQVLWG GDGAIVVKDR 

      1090       1100 
GTDRYLVIAN KDVKFIPPPK EIQKE 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60610 Unassigned DNA. Translation: AAA17529.1.

3D structure databases

ProteinModelPortalP23427.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.10.200. 1 hit.
2.30.30.10. 1 hit.
2.40.70.10. 1 hit.
3.30.420.10. 2 hits.
InterProIPR001969. Aspartic_peptidase_AS.
IPR008180. dUTP_pyroPase.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
PF00552. IN_DBD_C. 1 hit.
PF02022. Integrase_Zn. 1 hit.
PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
PF06815. RVT_connect. 1 hit.
PF06817. RVT_thumb. 1 hit.
[Graphical view]
SUPFAMSSF46919. SSF46919. 1 hit.
SSF50122. SSF50122. 1 hit.
SSF50630. SSF50630. 1 hit.
SSF53098. SSF53098. 2 hits.
PROSITEPS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS51027. INTEGRASE_DBD. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50876. ZF_INTEGRASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOL_VILV2
AccessionPrimary (citable) accession number: P23427
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 108 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