ID Q5RS65_9HIV1 Unreviewed; 300 AA.
AC Q5RS65;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Reverse transcriptase {ECO:0000313|EMBL:AAV57044.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AAV57044.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AAV57044.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAV57044.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA4378 {ECO:0000313|EMBL:AAV57044.1};
RX PubMed=15995959; DOI=10.1086/431601;
RA Rhee S.Y., Fessel W.J., Zolopa A.R., Hurley L., Liu T., Taylor J.,
RA Nguyen D.P., Slome S., Klein D., Horberg M., Flamm J., Follansbee S.,
RA Schapiro J.M., Shafer R.W.;
RT "HIV-1 Protease and reverse-transcriptase mutations: correlations with
RT antiretroviral therapy in subtype B isolates and implications for drug-
RT resistance surveillance.";
RL J. Infect. Dis. 192:456-465(2005).
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; AY801001; AAV57044.1; -; 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:AAV57044.1}; 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:AAV57044.1"
FT NON_TER 300
FT /evidence="ECO:0000313|EMBL:AAV57044.1"
SQ SEQUENCE 300 AA; 34729 MW; 85D6D12BA1A02D67 CRC64;
PISPIETVPV KLKPGMDGPR VKQWPLTEEK IKALMEICTE MEKEGKISKI GPENPYNTPI
FAIRKKNSTR WRKLVDFREL NKRTQDFWEV QLGIPHPAGL RKKKSVTILD VGDAYFSVPL
DPDFRKYTAF TIPSTNNETP GIRYQYNVLP QGWKGSPAIF QSSMTKILEP FRKQNPDLVI
YQYMDDLYVG SDLEIGQHRT KIEELRQHLL GWGFFTPDQK HQKEPPFLWM GYELHPDKWT
VQPIVLPEKD SWTVNDIXKL VGKLNWASQI YPGIXVRQLX KLLRGTKAXT EVVPLTEEAE
//
