ID E1AQP1_9HIV1 Unreviewed; 848 AA.
AC E1AQP1;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ADM89481.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ADM89481.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ADM89481.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADM89481.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Pt_45 {ECO:0000313|EMBL:ADM89481.1};
RX PubMed=20479206; DOI=10.1128/AAC.01720-09;
RA Ceccherini-Silberstein F., Van Baelen K., Armenia D., Trignetti M.,
RA Rondelez E., Fabeni L., Scopelliti F., Pollicita M., Van Wesenbeeck L.,
RA Van Eygen V., Dori L., Sarmati L., Aquaro S., Palamara G., Andreoni M.,
RA Stuyver L.J., Perno C.F.;
RT "Secondary integrase resistance mutations found in HIV-1 minority
RT quasispecies in integrase therapy-naive patients have little or no effect
RT on susceptibility to integrase inhibitors.";
RL Antimicrob. Agents Chemother. 54:3938-3948(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2; Evidence={ECO:0000256|ARBA:ARBA00000379};
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; HM990572; ADM89481.1; -; Genomic_RNA.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; 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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.200; -; 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; 2.30.30.10; Integrase, C-terminal domain superfamily, retroviral; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR017856; Integrase-like_N.
DR InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR InterPro; IPR001037; Integrase_C_retrovir.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR003308; Integrase_Zn-bd_dom_N.
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:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
DR Pfam; PF00552; IN_DBD_C; 1.
DR Pfam; PF02022; Integrase_Zn; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06815; RVT_connect; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR SUPFAM; SSF50122; DNA-binding domain of retroviral integrase; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS51027; INTEGRASE_DBD; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50876; ZF_INTEGRASE; 1.
PE 4: Predicted;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW DNA integration {ECO:0000256|ARBA:ARBA00022908};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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};
KW Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW Viral release from host cell {ECO:0000256|ARBA:ARBA00023113};
KW Virion maturation {ECO:0000256|ARBA:ARBA00023113};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00450}.
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 DOMAIN 563..604
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS50876"
FT DOMAIN 614..764
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 783..830
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS51027"
FT DNA_BIND 783..830
FT /note="Integrase-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00506"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADM89481.1"
FT NON_TER 848
FT /evidence="ECO:0000313|EMBL:ADM89481.1"
SQ SEQUENCE 848 AA; 96686 MW; 021234C64314CD1E CRC64;
PISSIETVPV KLKPGMDGPK VKQWPLTEEK IKALVEICTE MEREGKISKV GPENPYNTPV
FVIKKKDSTK WRKLVDFREL NKRTQDFWEV QLGIPHPSGL KKKKSVTVLD VGDAYFSVPL
DKDFRKYTAF TIPSINNETP GIRYQYNVLP QGWKGSPAIF QCGMTKILEP FRKQNPDIVI
YQYVDDLYVG SDLEIGQHRT KIKELREHLL KWGFTTPDKK HQKEPPFLWM GYELHPDKWT
VQPIVLPEKD SWTVNDIQKL VGKLNWASQI YPGIKVKQLC KLLRGTKALT DVIPLTKEAE
LELAENREIL KEPVHGVYYD PSKDLIAELQ KQGQGQWTYQ IYQEPFKNLK TGKYARMRGA
HTNDVKQLTE AVQKIATESI VIWGKTPKFK LPIQKETWEI WWTEYWQATW IPEWEFVNTP
PLVKLWYQLE KEPIMGAETF YVDGAANRET KSGKAGYVTN KGKQKVISLT DTTNQKTELH
AILLALQDSG LEVNIVTDSQ YALGVIHAQP DKSESELVSE IIEQLIKKEK VYLTWVPAHK
GIGGNEQVDK LVSNGIRKVL FLDGIDKAQE EHEKYHSNWR AMVSDFHLPP VVAKEIVASC
DKCQLKGEAM HGQVDCSPGI WQLDCTHLEG KVILVAVHVA SGYIEAEVIP AETGQETAYF
ILKLAGRWPV KTIHTDNGPN FISTAVKAAC WWAGIKQEFG IPYNPQSQGV VESMNKELKK
IIGQVRDQAE HLKTAVQMAV FIHNFKRKGG IGDYSAGERI IDIIATDIQT KELQKQITKI
QNFRVYYRDS RDPLWKGPAK LLWKGEGAVV IQDNSDIKVV PRRKAKIIRD YGKQMAGDDC
VASRQDED
//
