ID Q67D27_9HIV1 Unreviewed; 499 AA.
AC Q67D27;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AAS38114.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AAS38114.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AAS38114.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AAS38114.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=105848 {ECO:0000313|EMBL:AAS38114.1};
RX PubMed=15320992; DOI=10.1089/0889222041725172;
RA Gomez-Carrillo M., Quarleri J.F., Rubio A.E., Carobene M.G., Dilernia D.,
RA Carr J.K., Salomon H.;
RT "Drug resistance testing provides evidence of the globalization of HIV type
RT 1: a new circulating recombinant form.";
RL AIDS Res. Hum. Retroviruses 20:885-888(2004).
RN [2] {ECO:0000313|EMBL:AAS38114.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=105848 {ECO:0000313|EMBL:AAS38114.1};
RX PubMed=15585101; DOI=10.1089/aid.2004.20.1100;
RA Quarleri J.F., Rubio A., Carobene M., Turk G., Vignoles M., Harrigan R.P.,
RA Montaner J.S., Salomon H., Gomez-Carrillo M.;
RT "HIV type 1 BF recombinant strains exhibit different pol gene mosaic
RT patterns: descriptive analysis from 284 patients under treatment failure.";
RL AIDS Res. Hum. Retroviruses 20:1100-1107(2004).
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; AY365738; AAS38114.1; -; 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; -; 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 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; 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; 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; 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:AAS38114.1"
FT NON_TER 499
FT /evidence="ECO:0000313|EMBL:AAS38114.1"
SQ SEQUENCE 499 AA; 57052 MW; F1724CD3EFE59E17 CRC64;
PQITLWQRPL VTIKVGEQLT EALLDTGADN TVLEDIXLPG XWKPKXIGGI GGFIKVKQYD
NIXIEICGHK AIGTVLVGPT PVNIIGRDLL TQIGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALTEICTEM EKEGKISKIG PENPYNTPVF AIKKKNSTRW RKLVDFRELN
KRTQDFWEVQ LGIPHPAGLK RKKSVTVLDV GDAYFSVPLD KDFRKYTAFT IPSVNNETPG
IRYQYNVLPQ GWKGSPAIFQ SSMTRILEPF RKQNPDIVIY QYVDDLYVGS DLEIGQHRTK
IEELRQHLLK WGFTTPDEKH QKEPPFLWMG YELHPDKWTT QPIVLPEKDS WTVNDIQKLV
GKLNWASQIY PGIKVKQLCK LLRGTKALTE VIPLTKEAEL ELAENREILK EPVHGVYYDP
SKDLIVEIQK QGQGQWTYQI FQEPFKNLKT GKYARMRGAH TNDVKQLTEA VQKIATESIV
IWGKTPKFRL PILRETWDT
//
