ID A3FDH8_9HIV1 Unreviewed; 499 AA.
AC A3FDH8;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:ABN48185.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:ABN48185.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ABN48185.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ABN48185.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCCFE_HOMER_HIV_PRRT_1774 {ECO:0000313|EMBL:ABN48185.1};
RX PubMed=17616974; DOI=10.1371/journal.ppat.0030094;
RA Brumme Z.L., Brumme C.J., Heckerman D., Korber B.T., Daniels M.,
RA Carlson J., Kadie C., Bhattacharya T., Chui C., Szinger J., Mo T.,
RA Hogg R.S., Montaner J.S., Frahm N., Brander C., Walker B.D., Harrigan P.R.;
RT "Evidence of differential HLA class I-mediated viral evolution in
RT functional and accessory/regulatory genes of HIV-1.";
RL PLoS Pathog. 3:e94-e94(2007).
RN [2] {ECO:0000313|EMBL:ABN48185.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BCCFE_HOMER_HIV_PRRT_1774 {ECO:0000313|EMBL:ABN48185.1};
RA Brumme Z.L., Brumme C.J., Heckerman D., Korber B.T., Daniels M.,
RA Carlson J., Kadie C., Bhattacharya T., Chui C., Mo T., Hogg R.S.,
RA Montaner J.S.G., Frahm N., Brander C., Walker B.D., Harrigan P.;
RT "In vivo HLA class-I-associated polymorphisms in HIV-1 identified through a
RT genetic association approach correlate with clinical markers of immune
RT decline.";
RL Submitted (JAN-2007) 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; EF369084; ABN48185.1; -; Genomic_DNA.
DR MEROPS; A02.001; -.
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; -; 3.
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; IPR010659; RVT_connect.
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; PF06815; RVT_connect; 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:ABN48185.1"
FT NON_TER 499
FT /evidence="ECO:0000313|EMBL:ABN48185.1"
SQ SEQUENCE 499 AA; 57057 MW; 240D676DC1DE14C6 CRC64;
PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEISLPG RWKPKMIGGI GGFIKVRQYD
QICIEICGHK AIGTVLVGPT PVNIIGRNLL TQIGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALVEICTEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
KRTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD EDFRKYTAFT IPSTNNETPG
IRYQYNVLPQ GWKGSPAIFQ CSMTKILEPF RKQNPDXVIY QYMDDLYVGS DLEIGQHRTK
IEELRQHLLK WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIVLPEKDS WTVNDIQKLV
GKLNWASQIY PGIKVRQLCK LLRGTKALTE VXPLTXEAEL ELAENREILK EPVHGVYYDP
SKDLIAEIQK QGQGQWTYQI YQEPFKNLKT GKYARMRGAH TNDVKQLTEA VQKITTESIV
IWGKTPKFKL PIQKETWDT
//