ID D3XI95_9HIV1 Unreviewed; 434 AA.
AC D3XI95;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ADD11576.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ADD11576.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ADD11576.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADD11576.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21489016 {ECO:0000313|EMBL:ADD11576.1};
RX PubMed=20384495; DOI=10.5167/uzh-40523;
RA Kouyos R.D., von Wyl V., Yerly S., Boni J., Taffe P., Shah C.,
RA Burgisser P., Klimkait T., Weber R., Hirschel B., Cavassini M., Furrer H.,
RA Battegay M., Vernazza P.L., Bernasconi E., Rickenbach M., Ledergerber B.,
RA Bonhoeffer S., Gunthard H.F.;
RT "Molecular epidemiology reveals long-term changes in HIV type 1 subtype B
RT transmission in Switzerland.";
RL J. Infect. Dis. 201:1488-1497(2010).
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; GU344663; ADD11576.1; -; 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; 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 185
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:ADD11576.1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADD11576.1"
FT NON_TER 434
FT /evidence="ECO:0000313|EMBL:ADD11576.1"
SQ SEQUENCE 434 AA; 49393 MW; 3E9CCEED88B363CB CRC64;
PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEDINLPG RWKPKMIGGI GGFIKVRQYD
QIXXEIXGKK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALMEICXEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
KXTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD KXFRKYTAFT IPSINNETPG
IRYQYNVLPQ GWKGSPAIFQ CSMTKILEPF RRQNPDIVIY QYMDDLYVGS DLEXGQHRXK
IEELRQHLLK WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIVLPEKDS WTVNDIQKLV
GKLNWASQIY PGIKVRQLCK LLRGAKALTE VXPLTKEAEL ELAENREILK EPVHGVYYDP
SKNLIAEIQK QGLG
//
