ID Q5RRP2_9HIV1 Unreviewed; 350 AA.
AC Q5RRP2;
DT 21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Reverse transcriptase {ECO:0000313|EMBL:AAV57217.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AAV57217.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AAV57217.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAV57217.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CA41237 {ECO:0000313|EMBL:AAV57217.1};
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY801174; AAV57217.1; -; 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; IPR010659; RVT_connect.
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; PF06815; RVT_connect; 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:AAV57217.1}; 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:AAV57217.1"
FT NON_TER 350
FT /evidence="ECO:0000313|EMBL:AAV57217.1"
SQ SEQUENCE 350 AA; 40753 MW; A8B1511026748174 CRC64;
PISPIETVPV KLKPGMDGPR VKQWPLTXEK IKALVEICTE LEXEGKISKI GPENPYNTPI
FAIKKKNSTK WRKLMDFREL NKRTQDFWEV QLGIPHPAGL EKKKSVTVLD VGDAYFSIPL
DKDFRKYTAF TIPSTNNETP GIRYQYNVLP QGWKGSPAIF QSSMTKILEP FRKQNPDIVI
YQYVDDLYVG SDLEIGQHRT KIEELRHHLW RWGFYTPDKK HQKEPPFLWM GYELHPEKWT
VQPIVLPEKD SWTVNDIQKL VGKLNWASQI YAGIKVKQLC KLLRGTKALT EVIQLTEEAE
LELAENREIL KEPVHGVYYD PSKDLIAELQ KQGQGQWTYQ IYQEPFKNLK
//
