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Database: UniProt
Entry: E9P070_9HIV1
LinkDB: E9P070_9HIV1
Original site: E9P070_9HIV1 
ID   E9P070_9HIV1            Unreviewed;       396 AA.
AC   E9P070;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:ADV74392.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ADV74392.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ADV74392.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ADV74392.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=07NG.SN069 {ECO:0000313|EMBL:ADV74392.1};
RA   Etiebet M.-A., Carr J.K., Shepherd J., Gebi U., Ajayi S., Elegba O.,
RA   Iregbu K., Eyzaguirre L.M., Ndembi N., Peters S., Enzama R., Chang H.,
RA   Mondal P., Charurat M., Dakum P., Abimiku A., Blattner W.A.;
RT   "Tenofovir Disoproxil Fumarate based regimens associated with less
RT   nucleoside reverse transcriptase inhibitors drug resistance mutations in
RT   Nigerian patients failing first-line anti-retroviral therapy.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC       {ECO:0000256|RuleBase:RU004064}.
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DR   EMBL; HQ843514; ADV74392.1; -; 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:UniProtKB-KW.
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; -; 1.
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; IPR001969; Aspartic_peptidase_AS.
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   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   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU004064};
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, ECO:0000256|RuleBase:RU004064};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|RuleBase:RU004064};
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};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          76..145
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          199..389
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   REGION          10..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADV74392.1"
FT   NON_TER         396
FT                   /evidence="ECO:0000313|EMBL:ADV74392.1"
SQ   SEQUENCE   396 AA;  44926 MW;  A8435509C09F010F CRC64;
     FFRENLAFQQ GEARKLSPEQ TGTNSPTSRE LGNRRRGNHP PEAGTEGQGT ISSLNFPQIT
     LWQRPIVTVR IGGQLIEALL DTGADDTVLQ DINLQGKWKP KMIGGIGGFI KVRQYDQILI
     EIEGKKAIGT VLVGPTPVNI IGRNMLTQIG CTLNFPISPI XTVPVTLKPG MDGPXVKQWP
     LTEEKIKALT EICKEMEEEG KISKIGPENP YNTPVFAIKK KDSTKWRKLV DFRELNKRTQ
     DFWEVQLGIP HPAGLHKKKS VTVLDVGDAY FSVPLYEDFR KYTAFTIPSI NNETPGVRYQ
     YNVLPQGWKG SPAIFQASMT KILEPFRSQN PEIIIYQYVD DLYVASDLEI GQHRTKIEEL
     RNHLLKWGFT TPDKKHQKEP PFLWMGYELH PDKWTV
//
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