POL_HV1Z6
ID POL_HV1Z6 Reviewed; 148 AA.
AC P04586;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Gag-Pol polyprotein;
DE AltName: Full=Pr160Gag-Pol;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
DE Flags: Fragment;
GN Name=gag-pol;
OS Human immunodeficiency virus type 1 group M subtype D (isolate Z6) (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11708;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3036660; DOI=10.1016/0378-1119(87)90396-9;
RA Srinivasan A., Anand R., York D., Ranganathan P., Feorino P.,
RA Schochetman G., Curran J., Kalyanaraman V.S., Luciw P.A.,
RA Sanchez-Pescador R.;
RT "Molecular characterization of human immunodeficiency virus from Zaire:
RT nucleotide sequence analysis identifies conserved and variable domains in
RT the envelope gene.";
RL Gene 52:71-82(1987).
RN [2]
RP STRUCTURE BY NMR OF 80-130.
RX PubMed=7632683; DOI=10.1021/bi00031a002;
RA Lodi P.J., Ernst J.A., Kuszewski J., Hickman A.B., Engelman A., Craigie R.,
RA Clore G.M., Gronenborn A.M.;
RT "Solution structure of the DNA binding domain of HIV-1 integrase.";
RL Biochemistry 34:9826-9833(1995).
CC -!- FUNCTION: [Integrase]: Catalyzes viral DNA integration into the host
CC chromosome, by performing a series of DNA cutting and joining
CC reactions. This enzyme activity takes place after virion entry into a
CC cell and reverse transcription of the RNA genome in dsDNA. The first
CC step in the integration process is 3' processing. This step requires a
CC complex comprising the viral genome, matrix protein, Vpr and integrase.
CC This complex is called the pre-integration complex (PIC). The integrase
CC protein removes 2 nucleotides from each 3' end of the viral DNA,
CC leaving recessed CA OH's at the 3' ends. In the second step, the PIC
CC enters cell nucleus. This process is mediated through integrase and Vpr
CC proteins, and allows the virus to infect a non dividing cell. This
CC ability to enter the nucleus is specific of lentiviruses, other
CC retroviruses cannot and rely on cell division to access cell
CC chromosomes. In the third step, termed strand transfer, the integrase
CC protein joins the previously processed 3' ends to the 5' ends of
CC strands of target cellular DNA at the site of integration. The 5'-ends
CC are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-
CC shaped, gapped, recombination intermediate results, with the 5'-ends of
CC the viral DNA strands and the 3' ends of target DNA strands remaining
CC unjoined, flanking a gap of 5 bp. The last step is viral DNA
CC integration into host chromosome. This involves host DNA repair
CC synthesis in which the 5 bp gaps between the unjoined strands are
CC filled in and then ligated. Since this process occurs at both cuts
CC flanking the HIV genome, a 5 bp duplication of host DNA is produced at
CC the ends of HIV-1 integration. Alternatively, Integrase may catalyze
CC the excision of viral DNA just after strand transfer, this is termed
CC disintegration. {ECO:0000250|UniProtKB:P04585}.
CC -!- SUBUNIT: [Integrase]: Homotetramer; may further associate as a
CC homohexadecamer (By similarity). Part of the pre-integration complex
CC (PIC) which is composed of viral genome, matrix protein, Vpr and
CC integrase. Interacts with human SMARCB1/INI1 and human PSIP1/LEDGF
CC isoform 1. Interacts with human KPNA3; this interaction might play a
CC role in nuclear import of the pre-integration complex (By similarity).
CC Interacts with human NUP153; this interaction might play a role in
CC nuclear import of the pre-integration complex (By similarity).
CC {ECO:0000250|UniProtKB:P03367, ECO:0000250|UniProtKB:P04585,
CC ECO:0000250|UniProtKB:P12497}.
CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature
CC proteins. {ECO:0000250}.
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DR EMBL; K03458; AAA45376.1; -; Genomic_RNA.
DR PIR; A26192; A26192.
DR PDB; 1IHV; NMR; -; A/B=80-130.
DR PDB; 1IHW; NMR; -; A/B=80-130.
DR PDBsum; 1IHV; -.
DR PDBsum; 1IHW; -.
DR SMR; P04586; -.
DR MEROPS; A02.001; -.
DR EvolutionaryTrace; P04586; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR InterPro; IPR001037; Integrase_C_retrovir.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00552; IN_DBD_C; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS51027; INTEGRASE_DBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; AIDS; DNA integration; DNA recombination; DNA-binding;
KW Endonuclease; Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus;
KW Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW Lipid-binding; Magnesium; Metal-binding; Nuclease; Nucleotidyltransferase;
KW Transferase; Viral genome integration; Virus entry into host cell.
FT CHAIN <1..148
FT /note="Gag-Pol polyprotein"
FT /id="PRO_0000261289"
FT CHAIN <1..148
FT /note="Integrase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042448"
FT DOMAIN <1..64
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT DNA_BIND 83..130
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250|UniProtKB:P04585"
FT NON_TER 1
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1IHV"
FT STRAND 93..115
FT /evidence="ECO:0007829|PDB:1IHV"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1IHV"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1IHV"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1IHV"
SQ SEQUENCE 148 AA; 16840 MW; A0DD31618CF0FC0E CRC64;
IPYNPQSQGV VESMNKELKK IIGQVRDQAE HLKTAVQMAV FIHNFKRKGG IGGYSAGERI
IDIIATDIQT KELQKQITKI QNFRVYYRDS RDPIWKGPAK LLWKGEGAVV IQDNSDIKVV
PRRKVKIIRD YGKQMAGDDC VASRQDED
