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P16901 (POL_OMVVS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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
    EC=3.4.23.-
    Alternative name(s):
    Retropepsin
  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
OrganismOvine maedi visna related virus (strain South Africa) (SA-OMVV) (Ovine lentivirus)
Taxonomic identifier11664 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusOvine/caprine lentivirus group
Virus hostOvis aries (Sheep) [TaxID: 9940]

Protein attributes

Sequence length1086 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.

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 – 120120Protease By similarity
PRO_0000038853
Chain121 – 671551Reverse transcriptase/ribonuclease H By similarity
PRO_0000038854
Chain672 – 805134Deoxyuridine 5'-triphosphate nucleotidohydrolase By similarity
PRO_0000038855
Chain806 – 1086281Integrase By similarity
PRO_0000038856

Regions

Domain39 – 11072Peptidase A2
Domain167 – 356190Reverse transcriptase
Domain551 – 673123RNase H
Domain850 – 1010161Integrase catalytic
Zinc finger808 – 84942Integrase-type
DNA binding1027 – 107953Integrase-type

Sites

Active site441 By similarity

Sequences

Sequence LengthMass (Da)Tools
P16901 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 099F9614679FC8BD

FASTA1,086124,515
        10         20         30         40         50         60 
SNITAGKQQE GATCGAVRAP YVVTEAPPKI DIKVGTNWKK VLVDTGADRT IVRYHDNSGI 

        70         80         90        100        110        120 
PTGRIKLQGI GGIIEGEKWD KVVIQYKEKR IEGTIVVLPS SPVEVLGRDN MAKLDIGIIM 

       130        140        150        160        170        180 
ANLEEKKIPI TQVKLKEGCK GPHIAQWPLT QEKLEGLKEI VDKLEKEGKV GRAPPHWTCN 

       190        200        210        220        230        240 
TPIFCIKKKS GKWRMLIDFR ELNKQTEDLA EAQLGLPHPG GLQKKKHVTI LDIGDAYFTI 

       250        260        270        280        290        300 
PLYEPYRPYT CFTMLSPNNL GPCTRYYWKV LPQGWKLSPS VYQFTMQEIL RDWIAKHPMI 

       310        320        330        340        350        360 
QFGIYMDDIY IGSDLDIMKH REIVEELASY IAQYGFMLPE EKRQEGYPAK WLGFELHPEK 

       370        380        390        400        410        420 
WRFQKHTLPE IKEGTITLNK LQKLVGDLVW RQSLIGKSIP NILKLMEGDR ALQSERRIEL 

       430        440        450        460        470        480 
RHVKEWEECR RKLAEMEGNY YDEEKDVYGQ IDWGDKAIEY IVFQERGKPL WVNVVHNIKN 

       490        500        510        520        530        540 
LSQSQQIIKA AQKLTQEVII RIGKIPWILL PGKEEDWILE LQIGNITWMP SFWSCYRGSI 

       550        560        570        580        590        600 
RWKKRNVITE VVEGPTYYTD GGKKNGKGSL GFIASTGVKF RKHEEGTNQQ LELRAIEEAC 

       610        620        630        640        650        660 
KQGPEKMNIV TDSRYAYEFM RRNWDEEVIK NPIQARIMKL VHDKEQIGVH WVPGHKGIPQ 

       670        680        690        700        710        720 
NEEIDKYISE IFLAREGSGI LPKRAEDAGY DLICPQEVCI PAGQVRKIPI NLRINLKEDQ 

       730        740        750        760        770        780 
WAMVGTKSSF ASKGVFVQGG IIDSGYQGII QVVVYNSNDK EVIIPQGRKF AQLILMPLIH 

       790        800        810        820        830        840 
EDLEAWGETR RTERGNQGFG STGAYWIENI PLAEEDHSKW HQDAGSLHLD FGIPRTAAED 

       850        860        870        880        890        900 
IVQQCEVCQE NKMPSTIRGS NRRGIDHWQV DYTHYEDKII LVWVETNSGL IYAERVKGET 

       910        920        930        940        950        960 
GQEFRIMTIR WYGLFAPKSL QSDNGPAFVA EPTQLLMKYL GITHTTGIPW NPQSQALVER 

       970        980        990       1000       1010       1020 
THQTLKNTIE KFVSMFASFD SAIAAALITL NIKRKGGLGT SPMDIFIFNK EQQRIQQQST 

      1030       1040       1050       1060       1070       1080 
RNQSKFRFCY YRVRKRGHPG EWLGPTQVLW EGEGAIVIKD KNLEKYLVIA KKDVKFIPQP 


KEIQTE 

« Hide

References

[1]"Nucleotide sequence analysis of SA-OMVV, a visna-related ovine lentivirus: phylogenetic history of lentiviruses."
Querat G., Audoly G., Sonigo P., Vigne R.
Virology 175:434-447(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31646 Genomic RNA. Translation: AAA66812.1.

3D structure databases

ProteinModelPortalP16901.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSA02.006.

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_OMVVS
AccessionPrimary (citable) accession number: P16901
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 115 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