ID E0X7Q8_9HIV1 Unreviewed; 560 AA.
AC E0X7Q8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Reverse transcriptase {ECO:0000313|EMBL:ADM87074.1};
DE Flags: Fragment;
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ADM87074.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADM87074.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CR17-Apr09D {ECO:0000313|EMBL:ADM87074.1};
RX PubMed=20578518;
RA Jullaksorn D., Boonchawalit S., Uttiyoung J., Soonthornsata B., Yowang A.,
RA Krathong N., Chautrakul S., Ikuta K., Roobsoong A., Kanitvittaya S.,
RA Sawanpanyalert P., Kameoka M.;
RT "Sustained appearance of drug resistance-associated mutations in HIV-1
RT CRF01_AE protease and reverse transcriptase derived from protease
RT inhibitor-naive Thai patients.";
RL Southeast Asian J. Trop. Med. Public Health 41:347-357(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; GQ857270; ADM87074.1; -; 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:ADM87074.1}; 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:ADM87074.1"
FT NON_TER 560
FT /evidence="ECO:0000313|EMBL:ADM87074.1"
SQ SEQUENCE 560 AA; 64480 MW; 85B36169055BC21D CRC64;
PISPIDTVPV ALKPGMDGPK VKQWPLTEEK IKALTEICKE MEEEGKISKI GPENPYNTPI
FAIKKKDSTK WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKKKSVTVLD VGDAYFSVPL
DENFRKYTAF TIPSINNETP GVRYQYNVLP QGWKGSPAIF QSSMTKILEP FRIKNPEMVI
YQYMDDLYVG SDLEIGQHRA KIEELRAHLL SWGFTTPDKK HQKEPPFLWM GYELHPDRWT
VQPIELPEKD SWTVNDIQKL VGKLNWASQI YGGIKVKQLC KLLRGAKALT EVVPLTEEAE
LELAENREIL KTPVHGVYYD PSKDLVAEVQ KQGQDQWTYQ IYQEPFKNLK TGKYARKRSA
HTNDVRQLAE VVQKIATESI VIWGKTPKFR LPIQRETWET WWMEYWQATW IPEWEFVNTP
PLVKLWYQLE KDPIVGAETF YVDGAASRET KLGKAGYVTD RGRQKVVSLT ETTNQKTELH
AIHLALQDSG SEVNIVTDSQ YALGIIQAQP DRSESEVVNQ IIEELIKKEK VYLSWVPAHK
RIGGNEQVDR LVSSGIRKVL
//
