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Database: UniProt
Entry: Q90J70_9HIV1
LinkDB: Q90J70_9HIV1
Original site: Q90J70_9HIV1 
ID   Q90J70_9HIV1            Unreviewed;       402 AA.
AC   Q90J70;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   13-SEP-2023, entry version 116.
DE   SubName: Full=Pol polyprotein {ECO:0000313|EMBL:AAK35911.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:AAK35911.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:AAK35911.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AAK35911.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Shafer R., Gonzales M.J., Brun-Vezinet F.;
RT   "Online comparison of HIV-1 drug resistance algorithms identifies rates and
RT   causes of discordant interpretations.";
RL   Antivir. Ther. 6:101-101(2001).
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};
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DR   EMBL; AY031096; AAK35911.1; -; Genomic_RNA.
DR   PIR; A47330; A47330.
DR   PIR; C47330; C47330.
DR   PIR; F47330; F47330.
DR   PIR; S32132; S32132.
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:InterPro.
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; 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; INTEGRASE-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; PS50878; RT_POL; 1.
PE   4: Predicted;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
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};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022750};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023195}.
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:AAK35911.1"
FT   NON_TER         402
FT                   /evidence="ECO:0000313|EMBL:AAK35911.1"
SQ   SEQUENCE   402 AA;  45871 MW;  FABDD03F7D720DDC CRC64;
     PQITLWQRPL VTIKIGGQLK EALLDTGADN TVXEEMNLPG RWKPKXIGGI GGFIKVRQYD
     QVPIEICGHK AIGTVLIGPT PVNIIGRDLL TQLGCTLNFP ISPIETVPVK LKPGMDGPKV
     KQWPLTEEKI KALVEICTEL EKEGKISKIG PENPYNTPIF AIKKKDSTKW RKLVDFRELN
     KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD KDFRKYTAFT IPSVNNETPG
     IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPDIVIY QYVDDLYVGS DLEIGQHRAK
     IEELRQHLWK WGFYTPDKKH QKEPPFLWMG YELHPDKWTV QPIKLPEKDS WTVNDIQKLV
     GKLNWASQIY PGIKVRQLCK LLRGTKALTE VIPLTEEAEL EL
//
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