ID C7BD95_9HIV1 Unreviewed; 434 AA.
AC C7BD95;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ACT65366.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ACT65366.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ACT65366.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ACT65366.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZZQ453 {ECO:0000313|EMBL:ACT65366.1};
RG APIN Plus/Harvard PEPFAR Team;
RA Hawkins C., Chaplin B., Idoko J., Ekong E., Adewole I., Gashau W.,
RA Murphy R., Kanki P.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACT65366.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZZQ453 {ECO:0000313|EMBL:ACT65366.1};
RX PubMed=20964479; DOI=10.1089/aid.2010.0050;
RA Chaplin B., Eisen G., Idoko J., Onwujekwe D., Idigbe E., Adewole I.,
RA Gashau W., Meloni S., Sarr A.D., Sankale J.L., Ekong E., Murphy R.L.,
RA Kanki P.;
RT "Impact of HIV type 1 subtype on drug resistance mutations in Nigerian
RT patients failing first-line therapy.";
RL AIDS Res. Hum. Retroviruses 27:71-80(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 -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000256|RuleBase:RU004064}.
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DR EMBL; FJ931264; ACT65366.1; -; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; 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; cd05482; HIV_retropepsin_like; 1.
DR Gene3D; 3.30.70.270; -; 2.
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 InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
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; IPR000477; RT_dom.
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; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU004064};
KW DNA integration {ECO:0000256|ARBA:ARBA00023195};
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:ARBA00022771};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {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:ARBA00023195};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 20..89
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 143..333
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACT65366.1"
FT NON_TER 434
FT /evidence="ECO:0000313|EMBL:ACT65366.1"
SQ SEQUENCE 434 AA; 49475 MW; C1E81ABB025BF1E5 CRC64;
PQITLWQRPL VTVKIGGQII EALLDTGADD TVLEEINLPG RWKPKMIGGI GGFIKVRQYD
QILIEICGKK AIGTVLVGPT PVNIIGRNML TQIGCTLNFP ISPIETVPVK LKPGMDGPKI
KQWPLTEEKI KALKEICTEM EKEGKISKIG PENPYNTPIF AIKKKDSTRW RKLVDFRELN
KRTQDFWEVQ LGIPHPXGLE KKKSVTVLDV GDAYFSVPLD KDFRKYTAFT IPSXNNETPG
IRYQYNVLPQ GWKGSPAIFQ XSMTKILEPF RTKNPEVIIY QYVDDLYVAS DLEIGQHRAK
IEELREHLLK WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIELPEKDS WTVNDIQKLV
GKLNWASQIY AGIKVKQLCK LLRGAKALTD IVTLTEEAEL ELAENREILK EPVHGVYYDP
TKDLXAEVQK QGQD
//
