ID C8B412_9HIV1 Unreviewed; 301 AA.
AC C8B412;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE SubName: Full=Reverse transcriptase {ECO:0000313|EMBL:ACV14200.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACV14200.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACV14200.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACV14200.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA50863 {ECO:0000313|EMBL:ACV14200.1};
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; GQ208261; ACV14200.1; -; 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; INTEGRASE-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:ACV14200.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 44..234
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACV14200.1"
FT NON_TER 301
FT /evidence="ECO:0000313|EMBL:ACV14200.1"
SQ SEQUENCE 301 AA; 34579 MW; FF058D7C0E4CFDF6 CRC64;
PISPIETVPV XLKPGMDGPK VKQWPLTEEK IKALVEICTE MEKEGKISKI GPENPYNTPV
FAIKRKDGTK WRKLVDFREL NKXTQDFWEV QLGIPHPAGL KRKKSVTVLD VGDAYFSVPL
DXDFRKYTAF TIPSINNETP GIRYQYNVLP QGWKGSPAIF QSTMTKILEP FRNKNPXIEI
YQYVDDLYVG SDLEIGQHRT KIEELREHLL KWGFTTPDKK HQKEPPFLWM GYELHPDKWT
VQPITLPXKD SWTVNDIQKL VGKLNWASQI YPGIKVKQLC KLLKGAKALT EVVPLTTEAE
L
//