ID   A4UL07_9HIV1            Unreviewed;       299 AA.
AC   A4UL07;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:ABO71593.1};
DE   Flags: Fragment;
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ABO71593.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ABO71593.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=06ZA_PL174V2 {ECO:0000313|EMBL:ABO71593.1};
RX   PubMed=17272680; DOI=10.1093/molbev/msm021;
RA   Seoighe C., Ketwaroo F., Pillay V., Scheffler K., Wood N., Duffet R.,
RA   Zvelebil M., Martinson N., McIntyre J., Morris L., Hide W.;
RT   "A model of directional selection applied to the evolution of drug
RT   resistance in HIV-1.";
RL   Mol. Biol. Evol. 24:1025-1031(2007).
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; EF382284; ABO71593.1; -; Genomic_DNA.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.270; -; 2.
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; 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; PF00078; RVT_1; 1.
DR   Pfam; PF06817; RVT_thumb; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   4: Predicted;
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   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral release from host cell {ECO:0000256|ARBA:ARBA00023113};
KW   Virion maturation {ECO:0000256|ARBA:ARBA00023113}.
FT   DOMAIN          44..234
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABO71593.1"
FT   NON_TER         299
FT                   /evidence="ECO:0000313|EMBL:ABO71593.1"
SQ   SEQUENCE   299 AA;  34361 MW;  A4B690DA27A6596E CRC64;
     PISPIETVPV KLKPGMDGPK VKQWPLTEEK IKALTAICEE MEKEGKITKI GPENPYNTPV
     FAIKKKDSTX WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKXKSVTVLD VGDAYFSVPL
     DEGFRKYTAF TIPSINNETP GIRYQYNVLP QGWKGSPAIF QSSMIKILEP FREKNPEIVI
     XQYMDDLYVG SDLEIGPHRA KVEELREHLL RWGFTTPDKK HQKEPPFLWM GYELHPDKWT
     VQPIQLPEKE SWTVNDIQKL VGKLNWASQI YPGIKVRQLC KLLRGAKALT DIVPLTEEA
//