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Database: UniProt
Entry: B2MK81_9HIV1
LinkDB: B2MK81_9HIV1
Original site: B2MK81_9HIV1 
ID   B2MK81_9HIV1            Unreviewed;       404 AA.
AC   B2MK81;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:ACC51266.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ACC51266.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ACC51266.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACC51266.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=03-114339 {ECO:0000313|EMBL:ACC51266.1};
RX   PubMed=15567861; DOI=10.1126/science.1101786;
RA   Bonhoeffer S., Chappey C., Parkin N.T., Whitcomb J.M., Petropoulos C.J.;
RT   "Evidence for positive epistasis in HIV-1.";
RL   Science 306:1547-1550(2004).
RN   [2] {ECO:0000313|EMBL:ACC51266.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=03-114339 {ECO:0000313|EMBL:ACC51266.1};
RA   Bonhoeffer S., Chappey C., Parkin N.T., Whitcomb J.M., Petropoulos C.J.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
CC         cleavage modes: 1. sequence-specific internal cleavage of RNA. Human
CC         immunodeficiency virus type 1 and Moloney murine leukemia virus
CC         enzymes prefer to cleave the RNA strand one nucleotide away from the
CC         RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides
CC         from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides
CC         away from the primer terminus.; EC=3.1.26.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00023415};
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DR   EMBL; EU612751; ACC51266.1; -; Genomic_DNA.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR   CDD; cd05482; HIV_retropepsin_like; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001995; Peptidase_A2_cat.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR034170; Retropepsin-like_cat_dom.
DR   InterPro; IPR018061; Retropepsins.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR010661; RVT_thumb.
DR   PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR   PANTHER; PTHR41694:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
DR   Pfam; PF00077; RVP; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF06817; RVT_thumb; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   4: Predicted;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   DNA integration {ECO:0000256|ARBA:ARBA00023195};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022750};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW   Viral release from host cell {ECO:0000256|ARBA:ARBA00023113};
KW   Virion maturation {ECO:0000256|ARBA:ARBA00023113};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023195}.
FT   DOMAIN          20..89
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          143..333
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACC51266.1"
FT   NON_TER         404
FT                   /evidence="ECO:0000313|EMBL:ACC51266.1"
SQ   SEQUENCE   404 AA;  46083 MW;  8835B0F1B9AD03AD CRC64;
     PQITLWQRPI VTVKIGGQIK EALXDTGADD TXFEEMSLPG KWKPKLIGGI GGFLRVRQYD
     QIPIDICGHX TIGTVLVGPT PVNVIGRNLL TKIGCTLNFP ISPIETVPVK LKPGMDGPKV
     KQWPLTEEKI KALREICAEL EKEGKISKIG PENPYNTPVF AIKKKNSTKW RKLVDFRELN
     KRTQDFWEVQ LGIPHPAGLK KXKSVTVLDV GDAYFSVPLD KEFRKYTAFT IPSTNNETPG
     VRYQYNVLPQ GWKGSPAIFQ SSMTRILEPY RKQNPEIVIY QYVDDLYVGS DLEIGQHRTK
     VEELRQHLLK WGFFTPDKKH QXEHPFLWMG YELHPDKWTV QPIELPEKES WTVNDIQKLV
     GKLNWASQIY PGIKVRQLCK LIRGTKALTE VIPLTEEAEL ELAE
//
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