GenomeNet

Database: UniProt
Entry: G8HTH9_9HIV1
LinkDB: G8HTH9_9HIV1
Original site: G8HTH9_9HIV1 
ID   G8HTH9_9HIV1            Unreviewed;       434 AA.
AC   G8HTH9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:AER41711.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:AER41711.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:AER41711.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AER41711.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=052-2393-P-B {ECO:0000313|EMBL:AER41711.1};
RX   PubMed=21990420; DOI=10.1093/infdis/jir651;
RA   Eshleman S.H., Hudelson S.E., Redd A.D., Wang L., Debes R., Chen Y.Q.,
RA   Martens C.A., Ricklefs S.M., Selig E.J., Porcella S.F., Munshaw S.,
RA   Ray S.C., Piwowar-Manning E., McCauley M., Hosseinipour M.C., Kumwenda J.,
RA   Hakim J.G., Chariyalertsak S., de Bruyn G., Grinsztejn B., Kumarasamy N.,
RA   Makhema J., Mayer K.H., Pilotto J., Santos B.R., Quinn T.C., Cohen M.S.,
RA   Hughes J.P.;
RT   "Analysis of Genetic Linkage of HIV From Couples Enrolled in the HIV
RT   Prevention Trials Network 052 Trial.";
RL   J. Infect. Dis. 204:1918-1926(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JN634310; AER41711.1; -; 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; 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; 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   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:AER41711.1"
FT   NON_TER         434
FT                   /evidence="ECO:0000313|EMBL:AER41711.1"
SQ   SEQUENCE   434 AA;  49480 MW;  A7BD02BA78D66F38 CRC64;
     PQITLWQRPL VSIKVGGQTR EALLDTGADD TVLEXINLPG KWKPKMIGXI GGFIKVRQYD
     QITIEICGKK AIGAVLVGPT PVNIIGRNML TQLGCTLNFP ISPIETVPVK LKPGMDGPRV
     KQWPLTEEKI KALTEICEDM EKEGKITKIG PXNPYNTPVF AIKKKDSTKW RKLVDFRELN
     KRTQDFWEIQ LGIPHPSGLK KKRSVTVLDV GDAYFSVPLD ENFRKYTAFT IPSINNATPG
     IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RIKYPDIEIY QYMDDLYVGS DLEIGQHRAK
     IEELREHLLK WGLTTPDKKH QKEPPFLWMG YELHPDKWTV QPIQLPDKDS WTVNDIQKLV
     GKLNWASQIY PGIRVRHLCK LLRGAKALTD IVPLTEEAEL ELAENREIIK EPVHGVYYDP
     SKDLIAEVQK QGHD
//
DBGET integrated database retrieval system