ID Q5DNS5_9HIV1 Unreviewed; 560 AA.
AC Q5DNS5;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 29-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Reverse transcriptase {ECO:0000313|EMBL:AAT66798.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AAT66798.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AAT66798.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAT66798.1}
RP NUCLEOTIDE SEQUENCE.
RA Sundaravaradan V., Hahn T., Ahmad N.;
RT "Genetic Characterization of HIV Type 1 Reverse Transcriptase Gene From
RT Mothers and Infants Following Perinatal Transmission.";
RL Submitted (FEB-2004) 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; AY560407; AAT66798.1; -; Genomic_DNA.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.270; -; 3.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
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:SF5; RIBONUCLEASE H; 1.
DR Pfam; PF00075; RNase_H; 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 SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 4: Predicted;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW DNA integration {ECO:0000256|ARBA:ARBA00022908};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918,
KW ECO:0000313|EMBL:AAT66798.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 44..234
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 434..557
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAT66798.1"
FT NON_TER 560
FT /evidence="ECO:0000313|EMBL:AAT66798.1"
SQ SEQUENCE 560 AA; 64372 MW; F2C03CFCB0832A5A CRC64;
PISPIATVPV KLKPGMDGPK VKQWPLTEEK IKALVEICTE MEKEGKISKI GPENPYNTPV
FAIKKKDSTK WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKKKSVTVLD VGDAYFSVPL
DENFRKYTAF TIPSINNETP GIRYQYNALP QGWKGSPAIF QSSMTKILEP FRKQNPDIVI
YQYMDDLYVG SDLEIGQHRT KIEELRKHLL RWGLTTPDKK HQKEPPFLWM GYELHPDKWT
VQPIVLPEKD SWTVNDIQKL VGKLNWASQI YPGIKVKQLC KLLRGTKALT EVIPLTEEAE
LELAENREIL REPVHGVYYD PSKDLIAEIQ KQGYGQWTYQ IYQEPFKNLK TGKYARMRGA
HTNDVKQLTE AVQKISMESI VIWGKTPKFK LPIQKETWET WWIDYWQATW IPEWEFVNTP
PLVKLWYQLE KEPIAGAETF FVDGAANRET KLGKAGYVTD RGRQKVVSLT DTTNQKTELQ
AIHLALQDSG LEVNIVTDSQ YALGIIQAQP DKSESEIVNQ IIEQLVKKEK VYLAWVPAHK
GIGGNEQVDK LVSAGIRRVL
//
