ID E1APV8_9HIV1 Unreviewed; 848 AA.
AC E1APV8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ADM89198.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ADM89198.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ADM89198.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADM89198.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Pt_22 {ECO:0000313|EMBL:ADM89198.1};
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; HM990289; ADM89198.1; -; 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 CDD; cd01645; RT_Rtv; 1.
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:ADM89198.1"
FT NON_TER 848
FT /evidence="ECO:0000313|EMBL:ADM89198.1"
SQ SEQUENCE 848 AA; 96571 MW; A88C05DC17F01350 CRC64;
PISPIETVPV KLKPGMDGPK VKQWPLTEEK IKALVEICTE MEKEGKISRI GPENPYNTPV
FAIKKKDSTK WRKLVDFREL NKRTQDFWEV QLGIPHPAGL KKKKSVTVLD VGDAYFSVPL
DKDFRKYTAF TIPSTNNETP GIRYQYNVLP QGWKGSPAIF QCSMTKILEP FRKQNPDIVI
YQYMDDLYVG SDLEIGQHRT KIEELRNHLL KWGFTTPDKK HQKEPPFLWM GYELHPDKWT
VQPIMLPEKD SWTVNDIQKL VGKLNWASQI YPGIKVKQLC KLLRGTKALT EVVPLTEEAE
LELAENREIL KEPVHGVYYD PSKDLIAELQ KQGQGQWTYQ IYQEPFKNLK TGKYARVRSA
HTNDVKQLTE AVQKISTESI VIWGKTPKFK LPIQKETWEA WWMEYWQATW IPDWEFVNTP
PLVKLWYQLE KEPIVGAETF YVDGASNRET KLGKAGYVTD RGRQKVISLT DTTNQKTELQ
AINIALQDAG PEVNIVTDSQ YALGIIQAQP DKSESELVSQ IIEQLIKKEK VYLAWVPAHK
GIGGNEQVDK LVSAGIRKVL FLDGIDKAQE EHEKYHNNWR AMASDFNLPP VVAKEIVASC
DKCQLKGEAM HGQVDCNPGI WQLDCTHLEG KVILVAVHVA SGYIEAEVIP AETGQETAYF
ILKLAGRWPV KTIHTDNGGN FISATVKAAC WWAGIKQEFG IPYNPQSQGV VESMNKQLKQ
IIGQVRDQAE HLKTAVQMAV FIHNFKRKGG IGGYSAGERI VDIIASDIQT KELQKQITKI
QNFRVYYRDS RDPLWKGPAK LLWKGEGAVV IQDNSEIKVV PRRKAKIIRD YGKQMAGDDC
VASRQDED
//
