ID E2FCM8_9HIV1 Unreviewed; 306 AA.
AC E2FCM8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Reverse transcriptase {ECO:0000313|EMBL:ADN07410.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ADN07410.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ADN07410.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADN07410.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BREPM3597_07 {ECO:0000313|EMBL:ADN07410.1};
RX PubMed=20707640; DOI=10.1089/aid.2010.0023;
RA Teixeira D., Munerato P., Komninakis S.C., Fusuma E.E., Janini L.M.,
RA Sucupira M.C., Diaz R.S.;
RT "The detection of in vivo and in vitro HIV type 1 B/F profiles in Brazil
RT using a real-time PCR assay for five HIV type 1 genomic regions.";
RL AIDS Res. Hum. Retroviruses 26:981-990(2010).
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; HM118456; ADN07410.1; -; 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:ADN07410.1}; 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:ADN07410.1"
FT NON_TER 306
FT /evidence="ECO:0000313|EMBL:ADN07410.1"
SQ SEQUENCE 306 AA; 35303 MW; D33561C5BB3A5D39 CRC64;
PISPIETVPV KLKPGMDGPK VKQWPLTEEK IKALVEICTE MEKEGKISKI GPENPYNTPV
FAIKKKDSTK WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKKKSXTVLD VGDAYFSVPL
DEDFRKYTAF TIPSXNNETP GIRYQYNVLP QGWKGSPAIF QSSMTKILEP FRXQNPDIVI
YQYMDDLYVG SDLEIGQHRT KIEELRQHLL XWGFTTPDKK HQKEPPFLWM GYELHPDKWT
VQPIQLPEKD SWTVNDIQKL VGKLNWASQI YAGIKVKQLC KLLRGTKALT EVVPLTREAE
LELAEN
//
