ID Q99B08_9HIV1 Unreviewed; 562 AA.
AC Q99B08;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=Pol polyprotein {ECO:0000313|EMBL:AAK12221.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AAK12221.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AAK12221.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAK12221.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11429122; DOI=10.1089/088922201750252007;
RA Lukashov V.V., Huismans R., Jebbink M.F., Danner S.A., de Boer R.J.,
RA Goudsmit J.;
RT "Selection by AZT and rapid replacement in the absence of drugs of HIV type
RT 1 resistant to multiple nucleoside analogs.";
RL AIDS Res. Hum. Retroviruses 17:807-818(2001).
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; AF331346; AAK12221.1; -; 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 44..236
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 436..559
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAK12221.1"
FT NON_TER 562
FT /evidence="ECO:0000313|EMBL:AAK12221.1"
SQ SEQUENCE 562 AA; 64533 MW; 4711150BE9860FBF CRC64;
PISPIETVPV KLKPGMDGPK VKQWPLTEEK IKALVEICTE MEKEGKISKI GPENPYNTPV
FAIKKKSSSS GAWRKLVDFR ELNKRTQDFW EVQLGIPHPA GLKKKKSVTV LDVGDAYFSV
PLDKDFRKYT AFTIPSTNNE TPGIRYQYNV LPQGWKGSPA IFQCSMTKIL EPFRKQNPDI
VIYQYMDDLY VGSDLEIEQH RIKIEELREH LLKWGFYTPD KKHQKEPPFL WMGYELHPDK
WTVQPIQLPE KDSWTVNDLQ KLVGKLNWAS QIYAGIKVRQ LCKLLRGAKS LTEVVQLTEE
AELELAENRE ILKEPVHGVY YDPSKDLIAE VQKQGQGQWT YQIYQEPFKN LKTGKYARMK
GAHTNDVKPF TEAVQKIARE SIVIWGKTPK FKLPIQKETW EAWWTEYWQA TWIPEWEFVN
TPPLVKLWYQ LETEPIVGAE TFYVDGAANR ETKLGKAGYV TDKGRQKVVS ITDITNQKTE
LQAIHLALQD SGLEVNIVTD SQYALGIIQA QPDQSESELV SQIIEQLIKK EKVYLAWVPA
HKGIGGNEQV DKLVSAGIRK VL
//
