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}.
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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
//