ID A9YYS6_9HIV1 Unreviewed; 399 AA.
AC A9YYS6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 2.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Polyprotein {ECO:0000313|EMBL:ABY40860.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ABY40860.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ABY40860.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ABY40860.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=03HN_CR029 {ECO:0000313|EMBL:ABY40860.1};
RX PubMed=18366313; DOI=10.1089/aid.2007.0172;
RA Lloyd B., O'Connell R.J., Michael N.L., Aviles R., Palou E., Hernandez R.,
RA Cooley J., Jagodzinski L.L.;
RT "Prevalence of resistance mutations in HIV-1-Infected Hondurans at the
RT beginning of the National Antiretroviral Therapy Program.";
RL AIDS Res. Hum. Retroviruses 24:529-535(2008).
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; EU312643; ABY40860.1; -; Genomic_RNA.
DR MEROPS; A02.001; -.
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 UNSURE 382
FT /note="I or L"
FT /evidence="ECO:0000313|EMBL:ABY40860.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABY40860.1"
FT NON_TER 399
FT /evidence="ECO:0000313|EMBL:ABY40860.1"
SQ SEQUENCE 399 AA; 45401 MW; 53265B63CDC80349 CRC64;
PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMNLPG RWKPKMIGGI GGFIKVKQYD
QIAIEICGHK VIGTVLVGPT PVNIIGRNLL TQLGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALXEICTEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD KDFRKYTAFT IPSINNETPG
IRYQYNVLPQ GWKGSPAIFQ CSMTKILEPF RKQNPDIVIY QYMDDLYVGS DLETGQHRTK
IEELRQHLLK WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIVLPEKDS WTVNDIQKLV
GKLNWASQIY PGIKVKQLCK LLRGTKALTE VVPLTEEAE
//
