ID G5CGD5_9HIV1 Unreviewed; 499 AA.
AC G5CGD5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Pol protein {ECO:0000313|EMBL:AEQ01579.1};
DE Flags: Fragment;
GN Name=pol {ECO:0000313|EMBL:AEQ01579.1};
OS Human immunodeficiency virus 1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AEQ01579.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AEQ01579.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=76496 {ECO:0000313|EMBL:AEQ01579.1};
RX PubMed=21921202; DOI=10.1093/infdis/jir550;
RG UK HIV Drug Resistance Collaboration;
RA Leigh Brown A.J., Lycett S.J., Weinert L., Hughes G.J., Fearnhill E.,
RA Dunn D.T.;
RT "Transmission Network Parameters Estimated From HIV Sequences for a
RT Nationwide Epidemic.";
RL J. Infect. Dis. 204:1463-1469(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; JN101179; AEQ01579.1; -; 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; -; 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:SF5; RIBONUCLEASE H; 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:AEQ01579.1"
FT NON_TER 499
FT /evidence="ECO:0000313|EMBL:AEQ01579.1"
SQ SEQUENCE 499 AA; 57095 MW; E4CE9EC61683924A CRC64;
PQITLWQRPL VTIKIGGQLK EALLDTGADD TVLEEMHLPG RWKPKMIGGI GGFIKVKQYD
QISIEICGHK AIGTVLXGPT PVNIIGRNLL TQIGCTLNFP ISPIETVPVK LKPGMDGPKV
KQWPLTEEKI KALXEICTEM EKEGKISKIG PENPYNTPVF AIKKKDSTKW RKLVDFRELN
KXTQDFWEVQ LGIPHPAGLK KKKSVTVLDV GDAYFSVPLD XEFRKYTAFT IPSXNNETPG
IRYQYNVLPQ GWKGSPAIFQ SSMTKILEPF RKQNXDIVIY QYMDDLYVGS DLEIGQHRTK
IEELRQHLLR WGFTTPDKKH QKEPPFLWMG YELHPDKWTV QPIVLPEKDS WTVNDIQKLV
GKLNWASQIY PGIKVRQLCK LLRGXKALTD VIPLTEEAEL ELAENREILK EPVHGVYYDP
SKDLIAEIQK QGQGQWTYQI YQEPFKNLKT GKYAKMRGAH TNDVRQLTEA VQKITTESIV
IWGKAPKFKL PIQKETWET
//
