VINT_BPHC1
ID VINT_BPHC1 Reviewed; 337 AA.
AC P21442;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 02-JUN-2021, entry version 110.
DE RecName: Full=Integrase;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P36932};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P36932};
GN Name=int;
OS Haemophilus phage HP1 (strain HP1c1) (Bacteriophage HP1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Peduovirinae; Hpunavirus.
OX NCBI_TaxID=1289570;
OH NCBI_TaxID=727; Haemophilus influenzae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2546915; DOI=10.1128/jb.171.8.4232-4240.1989;
RA Goodman S.D., Scocca J.J.;
RT "Nucleotide sequence and expression of the gene for the site-specific
RT integration protein from bacteriophage HP1 of Haemophilus influenzae.";
RL J. Bacteriol. 171:4232-4240(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7997180; DOI=10.1111/j.1365-2958.1994.tb00462.x;
RA Esposito D., Scocca J.J.;
RT "Identification of an HP1 phage protein required for site-specific
RT excision.";
RL Mol. Microbiol. 13:685-695(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8710508; DOI=10.1093/nar/24.12.2360;
RA Esposito D., Fitzmaurice W.P., Benjamin R.C., Goodman S.D., Waldman A.S.,
RA Scocca J.J.;
RT "The complete nucleotide sequence of bacteriophage HP1 DNA.";
RL Nucleic Acids Res. 24:2360-2368(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9108478; DOI=10.1016/s0092-8674(00)80202-0;
RA Hickman A.B., Waninger S., Scocca J.J., Dyda F.;
RT "Molecular organization in site-specific recombination: the catalytic
RT domain of bacteriophage HP1 integrase at 2.7-A resolution.";
RL Cell 89:227-237(1997).
CC -!- FUNCTION: Integrase is necessary for integration of the phage into the
CC host genome by site-specific recombination. In conjunction with
CC excisionase, integrase is also necessary for excision of the prophage
CC from the host genome.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. {ECO:0000305}.
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DR EMBL; U24159; AAB09182.1; -; Genomic_DNA.
DR PIR; A33857; RSBPHP.
DR RefSeq; NP_043466.1; NC_001697.1.
DR PDB; 1AIH; X-ray; 2.50 A; A/B/C/D=168-337.
DR PDBsum; 1AIH; -.
DR SMR; P21442; -.
DR GeneID; 1261146; -.
DR KEGG; vg:1261146; -.
DR EvolutionaryTrace; P21442; -.
DR Proteomes; UP000001713; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase 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: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; 1.10.150.130; -; 1.
DR Gene3D; 1.10.443.10; -; 1.
DR InterPro; IPR044068; CB.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR013762; Integrase-like_cat_sf.
DR InterPro; IPR002104; Integrase_catalytic.
DR InterPro; IPR010998; Integrase_recombinase_N.
DR Pfam; PF00589; Phage_integrase; 2.
DR SUPFAM; SSF56349; SSF56349; 1.
DR PROSITE; PS51900; CB; 1.
DR PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA integration; DNA recombination; DNA-binding; Hydrolase;
KW Reference proteome; Transferase; Viral genome integration;
KW Virus entry into host cell.
FT CHAIN 1..337
FT /note="Integrase"
FT /id="PRO_0000197510"
FT DOMAIN 60..147
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 169..328
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 315
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:1AIH"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1AIH"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:1AIH"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:1AIH"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1AIH"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:1AIH"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1AIH"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:1AIH"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:1AIH"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:1AIH"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1AIH"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:1AIH"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:1AIH"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:1AIH"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:1AIH"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:1AIH"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:1AIH"
SQ SEQUENCE 337 AA; 38598 MW; D66C28425899D1A1 CRC64;
MAVRKDTKNG KWLAEVYVNG NASRKWFLTK GDALRFYNQA KEQTTSAVDS VQVLESSDLP
ALSFYVQEWF DLHGKTLSDG KARLAKLKNL CSNLGDPPAN EFNAKIFADY RKRRLDGEFS
VNKNNPPKEA TVNREHAYLR AVFNELKSLR KWTTENPLDG VRLFKERETE LAFLYERDIY
RLLAECDNSR NPDLGLIVRI CLATGARWSE AETLTQSQVM PYKITFTNTK SKKNRTVPIS
KELFDMLPKK RGRLFNDAYE SFENAVLRAE IELPKGQLTH VLRHTFASHF MMNGGNILVL
KEILGHSTIE MTMRYAHFAP SHLESAVKFN PLSNPAQ
