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P33459 (POL_CAEVC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pol polyprotein

Cleaved into the following 3 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. Integrase
    Short name=IN
Gene names
Name:pol
OrganismCaprine arthritis encephalitis virus (strain Cork) (CAEV-Co)
Taxonomic identifier11661 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusOvine/caprine lentivirus group
Virus hostCapra hircus (Goat) [TaxID: 9925]

Protein attributes

Sequence length1109 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.

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

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins.

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.

Sequence caution

The sequence AAA91826.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Protease
PRO_0000038829
Chain153 – 865713Reverse transcriptase/ribonuclease H
PRO_0000038830
Chain866 – 1109244Integrase
PRO_0000038831

Regions

Domain63 – 13472Peptidase A2
Domain191 – 380190Reverse transcriptase
Domain575 – 697123RNase H
Domain874 – 1034161Integrase catalytic
Zinc finger832 – 87342Integrase-type
DNA binding1051 – 110353Integrase-type

Sites

Active site681 By similarity

Sequences

Sequence LengthMass (Da)Tools
P33459 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 97B2F4B370B03CF3

FASTA1,109127,678
        10         20         30         40         50         60 
TRNHMSQLWK ERTYAKRMQR KERHKGKTAG KREEGDTCGA VRSSYGITSA PPMVQVRIGS 

        70         80         90        100        110        120 
QQRNLLFDTG ADRTIVRWHE GSGNPAGRIK LQGIGGIVEG EKWNNVELEY KGETRKGTIV 

       130        140        150        160        170        180 
VLPQSPVEVL GRDNMARFGI KIIMANLEEK RIPITKVKLK EGCTGPHVPQ WPLTEEKLKG 

       190        200        210        220        230        240 
LTEIIDKLVE EGKLGKAPPH WTCNTPIFCI KKKSGKWRML IDFRELNKQT EDLTEAQLGL 

       250        260        270        280        290        300 
PHPGGLQKKK HVTILDIGDA YFTIPLYEPY REYTCFTLLS PNNLGPCKRY YWKVLPQGWK 

       310        320        330        340        350        360 
LSPSVYQFTM QEILEDWIQQ HPEIQFGIYM DDIYIGSDLE IKKHREIVKD LANYIAQYGF 

       370        380        390        400        410        420 
TLPEEKRQKG YPAKWLGFEL HPQTWKFQKH TLPELTKGTI TLNKLQKLVG ELVWRQSIIG 

       430        440        450        460        470        480 
KSIPNILKLM EGDRELQSER KIEEVHVKEW EACRKKLEEM EGNYYNKDKD VYGQLAWGDK 

       490        500        510        520        530        540 
AIEYIVYQEK GKPLWVNVVH NIKNLSIPQQ VIKAAQKLTQ EVIIRTGKIP WILLPGKEED 

       550        560        570        580        590        600 
WRLELQLGNI TWMPKFWSCY RGHTRWRKRN IIEEVVEGPT YYTDGGKKNK VGSLGFIVST 

       610        620        630        640        650        660 
GEKFRKHEEG TNQQLELRAI EEALKQGPQT MNLVTDSRYA FEFLLRNWDE EVIKNPIQAR 

       670        680        690        700        710        720 
IMEIAHKKDR IGVHWVPGHK GIPQNEEIDK YISEIFLAKE GEGILPKREE DAGYDLICPE 

       730        740        750        760        770        780 
EVTIEPGQVK CIPIELRLNL KKSQWAMIAT KSSMAAKGVF TQGGIIDSGY QGQIQVIMYN 

       790        800        810        820        830        840 
SNKIAVVIPQ GRKFAQLILM DKKHGKLEPW GESRKTERGE KGFGSTGMYW IENIPLAEED 

       850        860        870        880        890        900 
HTKWHQDARS LHLEFEIPRT AAEDIVNQCE ICKEARTPAV IRGGNKRGVN HWQVDYTHYE 

       910        920        930        940        950        960 
NIILLVWVET NSGLIYAEKV KGESGQEFRI KVMHWYALFG PESLQSDNGP AFAAEPTQLL 

       970        980        990       1000       1010       1020 
MQYLGVKHTT GIPWNPQSQA IVERAHQLLK STLKKFQPQF VAVESAIAAA LVAINIKRKG 

      1030       1040       1050       1060       1070       1080 
GLGTSPMDIF IYNKEQKRIN NKYNKNSQKI QFCYYRIRKR GHQESGKDQP RYCGKGKEPI 

      1090       1100 
VVKDIESEKY LVIPYKDAKF IPPPTKEKE 

« Hide

References

[1]"Nucleotide sequence and transcriptional analysis of molecular clones of CAEV which generate infectious virus."
Saltarelli M., Querat G., Konings D.A.M., Vigne R., Clements J.E.
Virology 179:347-364(1990) [PubMed: 2171210] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33677 Genomic RNA. Translation: AAA91826.1. Different initiation.
PIRB45345.

3D structure databases

ProteinModelPortalP33459.
ModBaseSearch...

Protein family/group databases

MEROPSA02.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR008180. 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.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RVT.
IPR010659. RVT_connect.
IPR010661. RVT_thumb.
[Graphical view]
Gene3DG3DSA:1.10.10.200. Intgrase_N_Zn_bd. 1 hit.
G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
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. Integrase_Zn_N. 1 hit.
SSF50630. Pept_Aspartic. 1 hit.
SSF53098. RNaseH_fold. 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_CAEVC
AccessionPrimary (citable) accession number: P33459
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 14, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families