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Database: UniProt
Entry: XERC_ANOFW
LinkDB: XERC_ANOFW
Original site: XERC_ANOFW 
ID   XERC_ANOFW              Reviewed;         300 AA.
AC   B7GGC7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Tyrosine recombinase XerC {ECO:0000255|HAMAP-Rule:MF_01808};
GN   Name=xerC {ECO:0000255|HAMAP-Rule:MF_01808}; OrderedLocusNames=Aflv_1748;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1;
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
CC   -!- FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing
CC       the cutting and rejoining of the recombining DNA molecules. The XerC-
CC       XerD complex is essential to convert dimers of the bacterial chromosome
CC       into monomers to permit their segregation at cell division. It also
CC       contributes to the segregational stability of plasmids.
CC       {ECO:0000255|HAMAP-Rule:MF_01808}.
CC   -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC       molecules of XerC and two molecules of XerD. {ECO:0000255|HAMAP-
CC       Rule:MF_01808}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01808}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01808}.
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DR   EMBL; CP000922; ACJ34109.1; -; Genomic_DNA.
DR   RefSeq; WP_006323038.1; NC_011567.1.
DR   AlphaFoldDB; B7GGC7; -.
DR   SMR; B7GGC7; -.
DR   STRING; 491915.Aflv_1748; -.
DR   GeneID; 7038001; -.
DR   KEGG; afl:Aflv_1748; -.
DR   eggNOG; COG4974; Bacteria.
DR   HOGENOM; CLU_027562_9_0_9; -.
DR   Proteomes; UP000000742; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006313; P:DNA transposition; IEA:UniProtKB-UniRule.
DR   CDD; cd00798; INT_XerDC_C; 1.
DR   Gene3D; 1.10.150.130; -; 1.
DR   Gene3D; 1.10.443.10; Intergrase catalytic core; 1.
DR   HAMAP; MF_01808; Recomb_XerC_XerD; 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; IPR011931; Recomb_XerC.
DR   InterPro; IPR011932; Recomb_XerD.
DR   InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR   NCBIfam; TIGR02224; recomb_XerC; 1.
DR   NCBIfam; TIGR02225; recomb_XerD; 1.
DR   PANTHER; PTHR30349:SF41; INTEGRASE_RECOMBINASE HI_1414-RELATED; 1.
DR   PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR   Pfam; PF02899; Phage_int_SAM_1; 1.
DR   Pfam; PF00589; Phage_integrase; 1.
DR   SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR   PROSITE; PS51900; CB; 1.
DR   PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW   DNA integration; DNA recombination; DNA-binding; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Tyrosine recombinase XerC"
FT                   /id="PRO_1000187581"
FT   DOMAIN          2..88
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01248"
FT   DOMAIN          109..294
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01246"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
FT   ACT_SITE        281
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01808"
SQ   SEQUENCE   300 AA;  34736 MW;  738BEA66B887F75B CRC64;
     MENVNFTLNL FIEYLQIEKN YSEYTIACYK HDIGEFFEFM EREQIKQLQQ VSYSDVRLFL
     TELHQRKQSS RSIARKMSSL RSFYKFLLRE KIVSENPFAL ASLPKKEQKI PHFLYPDELE
     QLFVVNDLNT AIGQRNQAMI ELLYATGIRV SECCNIRLSH IDFSVCTILI SGKGNKQRYV
     PFGTYAKEAL ERYIQDGRQQ LASKAKTPTD VLFLNARGGA LTPRGVRHIL NDIVERAALS
     LKVSPHTFRH TFATHLLNEG ADLRSVQELL GHAHLSSTQV YTHVTKDHLR YVYLHSHPRA
//
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