ID B7TFC7_9HIV1 Unreviewed; 1006 AA.
AC B7TFC7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ACJ25934.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACJ25934.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACJ25934.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACJ25934.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SK174 {ECO:0000313|EMBL:ACJ25934.1};
RX PubMed=18596105; DOI=10.1128/JVI.00580-08;
RA Matthews P.C., Prendergast A., Leslie A., Crawford H., Payne R.,
RA Rousseau C., Rolland M., Honeyborne I., Carlson J., Kadie C., Brander C.,
RA Bishop K., Mlotshwa N., Mullins J.I., Coovadia H., Ndung'u T., Walker B.D.,
RA Heckerman D., Goulder P.J.;
RT "Central role of reverting mutations in HLA associations with human
RT immunodeficiency virus set point.";
RL J. Virol. 82:8548-8559(2008).
RN [2] {ECO:0000313|EMBL:ACJ25934.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SK174 {ECO:0000313|EMBL:ACJ25934.1};
RA Matthews P., Prendergast A., Goulder P.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
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; FJ199945; ACJ25934.1; -; Genomic_DNA.
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 CDD; cd01645; RT_Rtv; 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 79..148
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 202..392
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 592..715
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT DOMAIN 721..762
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS50876"
FT DOMAIN 772..922
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 941..988
FT /note="Integrase-type"
FT /evidence="ECO:0000259|PROSITE:PS51027"
FT DNA_BIND 941..988
FT /note="Integrase-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00506"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACJ25934.1"
FT NON_TER 1006
FT /evidence="ECO:0000313|EMBL:ACJ25934.1"
SQ SEQUENCE 1006 AA; 113712 MW; CB378A24330BA537 CRC64;
FFRENLAFPQ GEAGELPSEQ TRANSPTSGA NSSTNGELQV RGDNPRSEAG GERQGTLNFP
QITLWQRPLV TIKVGGQVKE ALLDTGADDT VLEEINLPGK WKPKMIGGIG GFINVRQYDQ
ILIEICGKKA IGTVLVGPTP VNIIGRNMLT QLGCTLNFPI SPIETVPVKL KPGMDGPKVK
QWPLTEEKIK ALTAICDEME KEGKISKIGP ENPYNTPIFA IKKKDSTKWR KLVDFRELNK
RTQDFWEVQL GIPHPAGLKK KKSVTVLDVG DAYFSVPLDE DFRKYTAFTI PSINNETPGI
RYQYNVLPQG WKGSPAIFQS SMTKILEPFR TQNPEIVIYQ YMDDLYVGSD LEIGQHRAKI
EELREHLLKW GFTTPDKKHQ KEPPFLWMGY ELHPDKWTVQ PIELPEKDSW TVNDIQKLVG
KLNWASQIYP GIKVRQLCKL LRGAKALTDI VPLTEEAELE LAENREILKE PVHGVYYDPS
KDLIAEIQKQ GHDQWTYQIY QEPFKNLKTG KYAKRRTAHT NDVKQLTEAV QKIAMESIVI
WGKTPKFRLP VQKETWETWW ADYWQATWIP EWEFINTPPL VKLWYQLEKE PIAGVETFYV
DGASNRETKI GKAGYVTDRG RQKVVTITET TNQKTELQAI QLALQDSGSE VNIVTDSQYA
LGIIQAKPDK SESELVNQII EELIKKERVY LSWVPAHKGI GGNEQVDKLV SSGIRKVLFL
DGIDKAQEEH EKYHSNWRAM ASEFNLPPIV AKEIVASCDK CQLKGEAMHG QVDCSPGIWQ
LDCTHLEGKV IIVAVHVASG YIEAEVIPAE TGQETAYYIL KLAGRWPVKV IHTDNGTNFT
STAVKAACWW AGIQQEFGIP YNPQSQGVVE SMNKELKKII GQVRDQAEHL KTAVQMAVFI
HNFKRKGGIG GYSAGERIID IIATDIQTKE LQKQIIKIQN FRVYYRDSRD PIWKGPAKLL
WKGEGAVVIQ DNSDIKVVPR RKVKIIRDYG KQMAGADCVA GRQDED
//
