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Database: UniProt
Entry: C9DL17_9HIV1
LinkDB: C9DL17_9HIV1
Original site: C9DL17_9HIV1 
ID   C9DL17_9HIV1            Unreviewed;       434 AA.
AC   C9DL17;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:ACW57900.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ACW57900.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ACW57900.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ACW57900.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=562454278341464 {ECO:0000313|EMBL:ACW57900.1};
RX   PubMed=19835478; DOI=10.1086/644505;
RA   Vercauteren J., Wensing A.M., van de Vijver D.A., Albert J., Balotta C.,
RA   Hamouda O., Kucherer C., Struck D., Schmit J.C., Asjo B., Bruckova M.,
RA   Camacho R.J., Clotet B., Coughlan S., Grossman Z., Horban A., Korn K.,
RA   Kostrikis L., Nielsen C., Paraskevis D., Poljak M., Puchhammer-Stockl E.,
RA   Riva C., Ruiz L., Salminen M., Schuurman R., Sonnerborg A., Stanekova D.,
RA   Stanojevic M., Vandamme A.M., Boucher C.A.;
RT   "Transmission of drug-resistant HIV-1 is stabilizing in Europe.";
RL   J. Infect. Dis. 200:1503-1508(2009).
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; GQ399763; ACW57900.1; -; Genomic_DNA.
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   CDD; cd01645; RT_Rtv; 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:ACW57900.1"
FT   NON_TER         434
FT                   /evidence="ECO:0000313|EMBL:ACW57900.1"
SQ   SEQUENCE   434 AA;  49181 MW;  87965386D18EEE16 CRC64;
     PQITLWQRPL VTVRIGGQLK EALLDTGADD TVLEEMSLPG RWKPKMIGGI GGFIKVRQYD
     QVSVEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP ISPIETVPVK LKPGMDGPKV
     KQWPLTEEKI KALTEICAEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
     KKTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD KDFRKYTAFT IPSTNNETPG
     IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNPDLVIY QYMDDLYVGS DLEIGQHRIK
     VEELRQHLLK WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPVVLPEKDS WTVNDIQKLV
     GKLNWASQIY PGIKVKQLCK LLRGTKALTE VIPLTAEAEL ELAENREILK EPVHGVYYDP
     SKDLIAEVQK QGQG
//
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