XERA_PYRAB
ID XERA_PYRAB Reviewed; 286 AA.
AC Q9V1P5; G8ZI16;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Tyrosine recombinase XerA {ECO:0000255|HAMAP-Rule:MF_02055, ECO:0000305};
GN Name=xerA {ECO:0000255|HAMAP-Rule:MF_02055, ECO:0000303|PubMed:20975945};
GN OrderedLocusNames=PYRAB03820; ORFNames=PAB0255;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=20975945; DOI=10.1371/journal.pgen.1001166;
RA Cortez D., Quevillon-Cheruel S., Gribaldo S., Desnoues N., Sezonov G.,
RA Forterre P., Serre M.C.;
RT "Evidence for a Xer/dif system for chromosome resolution in archaea.";
RL PLoS Genet. 6:E1001166-E1001166(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS), DNA-BINDING, FUNCTION, SUBUNIT,
RP MUTAGENESIS OF ARG-135 AND TYR-261, AND ACTIVE SITE.
RX PubMed=23667562; DOI=10.1371/journal.pone.0063010;
RA Serre M.C., El Arnaout T., Brooks M.A., Durand D., Lisboa J., Lazar N.,
RA Raynal B., van Tilbeurgh H., Quevillon-Cheruel S.;
RT "The carboxy-terminal alphaN helix of the archaeal XerA tyrosine
RT recombinase is a molecular switch to control site-specific recombination.";
RL PLoS ONE 8:E63010-E63010(2013).
CC -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC the cutting and rejoining of the recombining DNA molecules. Probably
CC involved in the resolution of chromosome dimers at the terminus of
CC replication. Binds to the dif site. {ECO:0000269|PubMed:20975945,
CC ECO:0000269|PubMed:23667562}.
CC -!- SUBUNIT: Homodimer in the absence of DNA substrate.
CC {ECO:0000269|PubMed:23667562}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02055,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02055, ECO:0000305}.
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DR EMBL; AJ248284; CAB49304.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69759.1; -; Genomic_DNA.
DR PIR; A75153; A75153.
DR RefSeq; WP_010867504.1; NC_000868.1.
DR PDB; 4A8E; X-ray; 2.99 A; A=1-286.
DR PDBsum; 4A8E; -.
DR AlphaFoldDB; Q9V1P5; -.
DR SMR; Q9V1P5; -.
DR STRING; 272844.PAB0255; -.
DR EnsemblBacteria; CAB49304; CAB49304; PAB0255.
DR GeneID; 1495272; -.
DR KEGG; pab:PAB0255; -.
DR PATRIC; fig|272844.11.peg.402; -.
DR eggNOG; arCOG01241; Archaea.
DR HOGENOM; CLU_027562_9_5_2; -.
DR OMA; HSFASHM; -.
DR OrthoDB; 57897at2157; -.
DR PhylomeDB; Q9V1P5; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009037; F:tyrosine-based site-specific recombinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006313; P:transposition, DNA-mediated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.130; -; 1.
DR Gene3D; 1.10.443.10; -; 1.
DR HAMAP; MF_02055; Recomb_XerA; 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 InterPro; IPR004107; Integrase_SAM-like_N.
DR InterPro; IPR033686; XerA.
DR Pfam; PF02899; Phage_int_SAM_1; 1.
DR Pfam; PF00589; Phage_integrase; 1.
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; Cytoplasm; DNA integration; DNA recombination; DNA-binding.
FT CHAIN 1..286
FT /note="Tyrosine recombinase XerA"
FT /id="PRO_0000095355"
FT DOMAIN 7..84
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT DOMAIN 100..274
FT /note="Tyr recombinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT ACT_SITE 135
FT /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT Rule:MF_02055, ECO:0000305|PubMed:23667562"
FT ACT_SITE 160
FT /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT Rule:MF_02055"
FT ACT_SITE 226
FT /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT Rule:MF_02055"
FT ACT_SITE 229
FT /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT Rule:MF_02055"
FT ACT_SITE 252
FT /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT Rule:MF_02055"
FT ACT_SITE 261
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A8P8, ECO:0000255|HAMAP-
FT Rule:MF_02055, ECO:0000305|PubMed:23667562"
FT MUTAGEN 135
FT /note="R->A: Lack of recombinase activity."
FT /evidence="ECO:0000269|PubMed:23667562"
FT MUTAGEN 261
FT /note="Y->F: Lack of recombinase activity."
FT /evidence="ECO:0000269|PubMed:23667562"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 27..43
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 66..83
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4A8E"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:4A8E"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:4A8E"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4A8E"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 171..182
FT /evidence="ECO:0007829|PDB:4A8E"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4A8E"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:4A8E"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:4A8E"
FT TURN 273..278
FT /evidence="ECO:0007829|PDB:4A8E"
SQ SEQUENCE 286 AA; 33025 MW; C44A99CB3F75A0E2 CRC64;
MEEREERVRD DTIEEFATYL ELEGKSRNTV RMYTYYISKF FEEGHSPTAR DALRFLAKLK
RKGYSTRSLN LVIQALKAYF KFEGLDSEAE KLKTPKMPKT LPKSLTEEEV RRIINAAETL
RDRLILLLLY GAGLRVSELC NLRVEDVNFE YGVIVVRGGK GGKDRVVPIS ESLLSEIKRY
LESRNDDSPY LFVEMKRKRK DKLSPKTVWR LVKKYGRKAG VELTPHQLRH SFATHMLERG
IDIRIIQELL GHSNLSTTQI YTKVSTKHLK EAVKKAKLVE SIIGGS
