ID F4YID9_9HIV1 Unreviewed; 560 AA.
AC F4YID9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AEA76551.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AEA76551.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AEA76551.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AEA76551.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=111773D {ECO:0000313|EMBL:AEA76551.1};
RX PubMed=21350368; DOI=10.1097/QAI.0b013e31820cf029;
RG AIDS Clinical Trials Group Study A5142 Protocol Team;
RA Brehm J.H., Lalama C.M., Hughes M.D., Haubrich R., Riddler S.A.,
RA Sluis-Cremer N., Mellors J.W.;
RT "Failure of initial therapy with two nucleosides and efavirenz is not
RT associated with early emergence of mutations in the C-terminus of HIV-1
RT reverse transcriptase.";
RL J. Acquir. Immune Defic. Syndr. 56:344-348(2011).
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; HM056553; AEA76551.1; -; 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 CDD; cd01645; RT_Rtv; 1.
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..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:AEA76551.1"
FT NON_TER 560
FT /evidence="ECO:0000313|EMBL:AEA76551.1"
SQ SEQUENCE 560 AA; 64438 MW; 82F6B0ECEC5F0D48 CRC64;
PISPIETVPV KLKPGMDGPK VKQWPLTEEK IKALVEICTE MEKEGKISKI GPENPYNTPV
FAIKKKDGXK WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKNKSVTVLD VGDAYFSVPL
DEDFRKYTAF TIPSINNETP GIRYQYNVLP QGWKGSPAIF QSSMTRILEP FRKNNPDIVI
YQYMDDLYVG SDLEIGQHRI KIEELRQHLL KWGFTTPDKK HQKEPPFLWM GYELHPDKWT
VQPIVLPDKD SWTVNDIQKL VGKLNWASQI YXGIKVXQLC KLLRGTKSLT EVIPLTEEAE
LELAENREIL KEPVHGVYYD PSKDLIAEIQ KQGDGQWTYQ IYQEPFKNLK TGKYARTRGT
HTNDVRQLTE AVQKIATESI VIWGRTPKFR LPIQKETWET WWTEYWQATW IPEWEFVNTP
PLVKLWYQLE KEPIVGAETF YVDGAANREN XLGKAGYVTD RGRQKVISIT DTTNQKTELQ
AIYLALQDSG PEVNVVTDSQ YALGIIQAQP DKSESELVSL IIEELIKKXK VYLAWVPAHK
GIGGNEQVDK LVSXGIRKVL
//
