ID K0H2H7_9HIV1 Unreviewed; 999 AA.
AC K0H2H7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AFU33110.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AFU33110.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AFU33110.1, ECO:0000313|Proteomes:UP000142244};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AFU33110.1, ECO:0000313|Proteomes:UP000142244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AA111a_WG9 {ECO:0000313|EMBL:AFU33110.1};
RX PubMed=22960785; DOI=10.1038/nature11519;
RA Rolland M., Edlefsen P.T., Larsen B.B., Tovanabutra S., Sanders-Buell E.,
RA Hertz T., de Camp A.C., Carrico C., Menis S., Magaret C.A., Ahmed H.,
RA Juraska M., Chen L., Konopa P., Nariya S., Stoddard J.N., Wong K., Zhao H.,
RA Deng W., Maust B.S., Bose M., Howell S., Bates A., Lazzaro M.,
RA O'Sullivan A., Lei E., Bradfield A., Ibitamuno G., Assawadarachai V.,
RA O'Connell R.J., de Souza M.S., Nitayaphan S., Rerks-Ngarm S., Robb M.L.,
RA McLellan J.S., Georgiev I., Kwong P.D., Carlson J.M., Michael N.L.,
RA Schief W.R., Gilbert P.B., Mullins J.I., Kim J.H.;
RT "Increased HIV-1 vaccine efficacy against viruses with genetic signatures
RT in Env V2.";
RL Nature 490:417-420(2012).
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};
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000256|RuleBase:RU004064}.
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DR EMBL; JX448067; AFU33110.1; -; Genomic_RNA.
DR Proteomes; UP000142244; Genome.
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; cd05482; HIV_retropepsin_like; 1.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 3.30.70.270; -; 3.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
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; IPR001969; Aspartic_peptidase_AS.
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; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
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; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06815; RVT_connect; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR SUPFAM; SSF50630; Acid proteases; 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; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
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 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU004064};
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, ECO:0000256|RuleBase:RU004064};
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, ECO:0000256|RuleBase:RU004064};
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 72..141
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 195..385
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 585..708
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT DOMAIN 714..755
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS50876"
FT DOMAIN 765..915
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 934..981
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS51027"
FT DNA_BIND 934..981
FT /note="Integrase-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00506"
FT REGION 9..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFU33110.1"
SQ SEQUENCE 999 AA; 113012 MW; B56425BE12F72589 CRC64;
FFRENLAFQG EARKFSPEQT GANSPTSRKL GDGGRDTEAG AERQGTSSSF NFPQITLWQR
PLVTVRIGGQ LIEALLDTGA DDTVLEEINL PGKWKPKMIG GIGGFIKVRQ YDQILIEICG
KKAIGTVLVG PTPVNIIGRN MLTQIGCTLN FPISPIDTVP VTLKPGMDGP KVKQWPLTEE
KIKALTEICK EMEEEGKISK IGPENPYNTP IFAIKKKDGT KWRKLVDFRE LNKRTQDFWE
VQLGIPHPAG LKKKKSVTVL DVGDAYFSVP XDESFRKYTA FTIPSTNNET PGIRYQYNVL
PQGWKGSPAI FQSSMTKILE PFRIKNPEMI IYQYMDDLYV GSDLDIGQHR AKIEELRAHL
LSWGFTTPDK KHQKEPPFLW MGYELHPDRW TVQPIELPEK DSWTVNDIQK LVGKLNWASQ
IYAGIKVKQL CKLLRGAKAL TDIVPLTEEA ELELAENREI LKTPVHGVYY DPSKELIAEV
QKQGQDQWTY QIYQEPFKNL KTGKYARKRS AHTNDVRQLT EVVQKIATES IVIWGKTPRF
RLPIQKETWE TWWMEYWQAT WIPEWEFVNT PPLVKLWYQL EKDPIAGAET FYVDGAASRE
TKLGKAGYVT DRGRQKVVSL TETTNQKTEL HAIHLALQDS GSEVNIVTDS QYALGIIXAQ
PDRSESEVVS QIIEELIKKD KVYLSWVPAH KGIGGNEQVD KLVSSGIRRV LFLDGIDKAQ
EEHERYHSNW RTLASDFNLP PIIAKEIVAS CDKCQVKGEA MHGQVDCSPG IWQLDCTHLE
GKVILVAVHV ASGYIEAEVI PAETGQETAY FLLKLAGRWP VKVIHTDNGS NFTSAAVKAA
CWWANVRQEF GIPYNPQSQG VVESMNKELK KIIGQVREQA EHLKTAVQMA VFIHNFKRKG
GIGGYSAGER IIDIIATDIQ TKELQKQITK IQNFRVYYRD SRDPIWKGPA KLLWKGEGAV
VIQDNNDIKV VPRRKAKIIR DYGKQMAGDD CVAGRQDED
//
