ID A0A316TF22_9ACTN Unreviewed; 346 AA.
AC A0A316TF22;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Tyrosine recombinase XerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN Name=xerC {ECO:0000256|HAMAP-Rule:MF_01808};
GN ORFNames=DJ010_17100 {ECO:0000313|EMBL:PWN01749.1};
OS Nocardioides silvaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2201891 {ECO:0000313|EMBL:PWN01749.1, ECO:0000313|Proteomes:UP000245507};
RN [1] {ECO:0000313|EMBL:PWN01749.1, ECO:0000313|Proteomes:UP000245507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2018079 {ECO:0000313|EMBL:PWN01749.1,
RC ECO:0000313|Proteomes:UP000245507};
RA Li C., Wang G.;
RT "Nocardioides silvaticus genome.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01808}.
CC -!- SUBUNIT: Forms a cyclic heterotetrameric complex composed of two
CC molecules of XerC and two molecules of XerD. {ECO:0000256|HAMAP-
CC Rule:MF_01808}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01808}.
CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01808}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWN01749.1}.
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DR EMBL; QGDD01000008; PWN01749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316TF22; -.
DR OrthoDB; 9801717at2; -.
DR Proteomes; UP000245507; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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; IPR023009; Tyrosine_recombinase_XerC/XerD.
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 SUPFAM; SSF47823; lambda integrase-like, N-terminal domain; 1.
DR PROSITE; PS51900; CB; 1.
DR PROSITE; PS51898; TYR_RECOMBINASE; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_01808};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_01808};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829, ECO:0000256|HAMAP-
KW Rule:MF_01808};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01808};
KW DNA integration {ECO:0000256|ARBA:ARBA00022908, ECO:0000256|HAMAP-
KW Rule:MF_01808};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_01808};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01808}; Reference proteome {ECO:0000313|Proteomes:UP000245507}.
FT DOMAIN 46..132
FT /note="Core-binding (CB)"
FT /evidence="ECO:0000259|PROSITE:PS51900"
FT DOMAIN 153..340
FT /note="Tyr recombinase"
FT /evidence="ECO:0000259|PROSITE:PS51898"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 221
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 292
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 295
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 318
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
FT ACT_SITE 327
FT /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01808"
SQ SEQUENCE 346 AA; 37632 MW; B85BE923D543894A CRC64;
MAVDRGRTGV RRPRRDLPRR PPCSSYDRGV TEDQAQRAEE GAFLPESLTR VLGDYERHLA
SERNLAPHTV KAYAGDIGGL LEHAHRLGFA DVSDLDLRTL RSWLAKQQTM GRSRTTLARR
ATAARVFTAW LARTGRATTD VGSALGSPKP HQTLPSVLRV DEAHELIASA TALADDGSPV
GLRDVAMLEL LYATGMRVGE LCGLDVDDVD RDRNVVRVFG KGRKERAVPF GQPAAAAIDA
WLTRGRGRLA RPGSGPALFL GARGGRIDQR AVRGLVHRRI ADVPGAPDLG PHGLRHTAAT
HLLEGGADLR SVQELLGHAS LATTQRYTHV TTERLRNAYR QAHPRA
//
