ID A7XA27_9HIV1 Unreviewed; 305 AA.
AC A7XA27;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Reverse transcriptase {ECO:0000313|EMBL:ABU89158.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ABU89158.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ABU89158.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ABU89158.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=01AOCSE117 {ECO:0000313|EMBL:ABU89158.1};
RX PubMed=18562253; DOI=10.1016/j.meegid.2008.05.003;
RA Bartolo I., Rocha C., Bartolomeu J., Gama A., Marcelino R., Fonseca M.,
RA Mendes A., Epalanga M., Silva P.C., Taveira N.;
RT "Highly divergent subtypes and new recombinant forms prevail in the
RT HIV/AIDS epidemic in Angola: new insights into the origins of the AIDS
RT pandemic.";
RL Infect. Genet. Evol. 9:672-682(2009).
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; EU068343; ABU89158.1; -; 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:ABU89158.1}; 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:ABU89158.1"
FT NON_TER 305
FT /evidence="ECO:0000313|EMBL:ABU89158.1"
SQ SEQUENCE 305 AA; 35013 MW; F18FD2F1CA982966 CRC64;
PISPIETVPV ALKPGMDGPR VKQWPLTEEK IKALKEICDE MEKEGKISKI GPENPYNTPI
FAIKKKDSTK WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKKKSVTVLD VGDAYFSVPL
DENFRKYTAF TIPSINNETP GIRYQYNVLP QGWKGSPAIF QSSMTKILEP FRAQNPEMVI
YQYMDDLYVG SDLEIGQHRA KIEELRAHLL SWGFTTPDKK HQKEPPFLWM GYELHPDKWT
VQPIQLPEKD SWTVNDIQKL VGKLNWASQI YPGIKVKQLC KLLKGAKALT DVVPLTEEAE
LELAE
//
