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Database: UniProt
Entry: D3JRZ2_9HIV1
LinkDB: D3JRZ2_9HIV1
Original site: D3JRZ2_9HIV1 
ID   D3JRZ2_9HIV1            Unreviewed;       434 AA.
AC   D3JRZ2;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Pol protein {ECO:0000313|EMBL:ADB79437.1};
DE   Flags: Fragment;
GN   Name=pol {ECO:0000313|EMBL:ADB79437.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:ADB79437.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:ADB79437.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=325 {ECO:0000313|EMBL:ADB79437.1};
RA   Seclen E., Gonzalez M.M., Corral A., De Mendoza C., Soriano V., Poveda E.;
RT   "High prevalence of natural polymorphisms in gag (CA-SP1) associated with
RT   reduced response to Bevirimat, an HIV-1 maturation inhibitor.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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; GU264328; ADB79437.1; -; 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   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADB79437.1"
FT   NON_TER         434
FT                   /evidence="ECO:0000313|EMBL:ADB79437.1"
SQ   SEQUENCE   434 AA;  49306 MW;  0C66C3A8FE5F9507 CRC64;
     PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEDMNLPG RWKPKXIGGI GGFIKVRQYD
     QIPIEICGHK AIGTVLVGPT PVNIIGRNLL TXIGCTLNXP ISPIETVPVK LKPGMDGPKV
     KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
     KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLY EDFRKYTAFT IPSTNNETPG
     IRYQYNVLPQ GWKGSPAIFQ ASMTKILEPF RKQNPDIVIY QYMDDLYVGS DLEIGQHRTK
     IEELRZHLLX WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIMLPEKDS WTVNDIQKLV
     GKLNWASQIY PGIKVRQLCK LLRGAKALTE VIPLTEEAEL ELAENREILX EPVHGVYYDP
     SKDLIAEIQK QGNG
//
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