ID   C8BBT0_9HIV1            Unreviewed;       301 AA.
AC   C8BBT0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Reverse transcriptase {ECO:0000313|EMBL:ACV15584.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ACV15584.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ACV15584.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACV15584.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CA58234 {ECO:0000313|EMBL:ACV15584.1};
RA   Shahriar R., Rhee S.-Y., Liu T.F., Fessel W.J., Scarsella A., Towner W.,
RA   Holmes S.P., Zolopa A.R., Shafer R.W.;
RT   "Nonpolymorphic HIV-1 Protease and RT Treatment-Selected Mutations.";
RL   Submitted (MAY-2009) 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; GQ210989; ACV15584.1; -; Genomic_RNA.
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   ECO:0000313|EMBL:ACV15584.1}; 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:ACV15584.1"
FT   NON_TER         301
FT                   /evidence="ECO:0000313|EMBL:ACV15584.1"
SQ   SEQUENCE   301 AA;  34807 MW;  FC6BF209AD664973 CRC64;
     PISPIETVPV KLKPGMDGPX VKQWPLTEEK IRALVEICTE LEKEGKISKI GPENPYNTPV
     FAIKKKDSTK WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKKKSVTVLD VGDAYFSVPL
     DKDFRKYTAF TIPSINNETP GIRYQYNVLP QGWKGSPAIF QSSMTKILEP FRKQNPDIVI
     YQYVDDLYVG SDLEIGQHRX KIEELRQHLL RWGFDTPDKK HQKEPPFXWM GYELHPDKWT
     VQPIXLPEKD SWTVNDIQKL VGKLNWASQI YAGIKVRQLC KLLRGTKSLT EVVPLTREAE
     L
//