ID D0U7Q3_9HIV1 Unreviewed; 518 AA.
AC D0U7Q3;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ACY07732.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACY07732.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACY07732.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACY07732.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CMNYU107 {ECO:0000313|EMBL:ACY07732.1};
RA Powell R.L.R., Nyambi P.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACY07732.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CMNYU107 {ECO:0000313|EMBL:ACY07732.1};
RX PubMed=20334562; DOI=10.1089/aid.2009.0174;
RA Powell R.L., Lezeau L., Kinge T., Nyambi P.N.;
RT "Longitudinal quasispecies analysis of viral variants in HIV type 1 dually
RT infected individuals highlights the importance of sequence identity in
RT viral recombination.";
RL AIDS Res. Hum. Retroviruses 26:253-264(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; GQ432955; ACY07732.1; -; Genomic_RNA.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..211
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 411..518
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACY07732.1"
FT NON_TER 518
FT /evidence="ECO:0000313|EMBL:ACY07732.1"
SQ SEQUENCE 518 AA; 59849 MW; E439B893D2985CFD CRC64;
WPLTEEKIKA LIEICTEMEK EGKISRIGPE NPYNTPIFAI KKKDSTKWRK LVDFRELNKR
TQDFWEVQLG IPHPAGLKKK KSVTVLDVGD AYFSVPLDES FRKYTAFTIP SINNETPGIR
YQYNVLPQGW KGSPAIFQCS MTKILEPFRI KNPEIVIYQY MDDLYVGSDL EIGQHRAKIE
ELREHLLSWG FTTPDKKHQK EPPFLWMGYE LHPDKWTVQP IQLPDKESWT VNDIQKLVGK
LNWASQIYAG IKVKQLCKLL RGAKALTDIV PLTAEAELEL AENREILKNP VHGVYYDPSK
ELIAEVQKQG LDQWTYQIYQ EPYKNLKTGK YAKRGAAHTN DVKQLTEVVQ KISTESIVIW
GKTPKFRLPI RKETWEVWWT EYWQATWIPD WEFVNTPPLV KLWYRLETEP IAGAETYYVD
GAASRETKLG KAGYVTDKGK QKIITLTDTT NQKTELHAIQ LALQDSGSEV NIVTDSQYAL
GIIQAQPDRS ESELVNQIIE QLIKKEKVYL SWVPAHKG
//
