ID G8IFZ5_9HIV1 Unreviewed; 404 AA.
AC G8IFZ5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AER35563.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AER35563.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AER35563.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AER35563.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HIV_PRRT_PJ01967_53 {ECO:0000313|EMBL:AER35563.1};
RX PubMed=21851324; DOI=10.1089/aid.2010.0355;
RA Myers J.E., Taylor B.S., Rojas Fermin R.A., Reyes E.V., Vaughan C.,
RA Jose L., Javier C., Franco Estevez R., Donastorg Cabral Y., Batista A.,
RA Lie Y., Coakley E., Hammer S.M., Brudney K.;
RT "Transmitted Drug Resistance Among Antiretroviral-Naive Patients with
RT Established HIV Type 1 Infection in Santo Domingo, Dominican Republic and
RT Review of the Latin American and Caribbean Literature.";
RL AIDS Res. Hum. Retroviruses 0:0-0(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; JN713619; AER35563.1; -; 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:AER35563.1"
FT NON_TER 404
FT /evidence="ECO:0000313|EMBL:AER35563.1"
SQ SEQUENCE 404 AA; 46167 MW; 682F63EDF9FEA226 CRC64;
PQITLWQRPL VTIKIEGQLK EALLDTGADD TVLEEXXLXG RWKPKMIGGI GGFIKVKQYD
QILVEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALXEICTEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
KRTQDFWEXQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD ENFRKYTAFT IPSXNNETPG
IRYQYNVLPQ GWKGSPAIFQ XSMTKILEPF RKQNPEXVIY QYMDDLYVGS DLEIXQHRTK
IEELRQHLLK WGFXTPDKKH QKEPPFLWMG YELHPDKWTV QPIVLPEKDS WTVNDIQKLV
GKLNWASQIY PGIKVKQLCR LIRGTKALTE VXPLTKEAEL ELAE
//
