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Database: UniProt
Entry: A0A1H7GHV6_9LACT
LinkDB: A0A1H7GHV6_9LACT
Original site: A0A1H7GHV6_9LACT 
ID   A0A1H7GHV6_9LACT        Unreviewed;       298 AA.
AC   A0A1H7GHV6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Tyrosine recombinase XerD {ECO:0000256|ARBA:ARBA00015810, ECO:0000256|HAMAP-Rule:MF_01807};
GN   Name=xerD {ECO:0000256|HAMAP-Rule:MF_01807};
GN   ORFNames=SAMN04488099_102133 {ECO:0000313|EMBL:SEK36060.1};
OS   Alkalibacterium pelagium.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=426702 {ECO:0000313|EMBL:SEK36060.1, ECO:0000313|Proteomes:UP000199081};
RN   [1] {ECO:0000313|Proteomes:UP000199081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19183 {ECO:0000313|Proteomes:UP000199081};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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_01807}.
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_01807}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01807}.
CC   -!- SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.
CC       {ECO:0000256|ARBA:ARBA00010450, ECO:0000256|HAMAP-Rule:MF_01807}.
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DR   EMBL; FNZU01000002; SEK36060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7GHV6; -.
DR   STRING; 426702.SAMN04488099_102133; -.
DR   Proteomes; UP000199081; 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   HAMAP; MF_01807; Recomb_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; IPR011932; Recomb_XerD.
DR   InterPro; IPR023009; Tyrosine_recombinase_XerC/XerD.
DR   NCBIfam; TIGR02225; recomb_XerD; 1.
DR   PANTHER; PTHR30349; PHAGE INTEGRASE-RELATED; 1.
DR   PANTHER; PTHR30349:SF87; PROPHAGE INTEGRASE INTD-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 {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   Chromosome partition {ECO:0000256|ARBA:ARBA00022829, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01807};
KW   DNA integration {ECO:0000256|ARBA:ARBA00022908, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_01807};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01807}; Reference proteome {ECO:0000313|Proteomes:UP000199081}.
FT   DOMAIN          1..86
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          107..292
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51898"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        247
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        279
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
SQ   SEQUENCE   298 AA;  34586 MW;  6667A03285EB8F38 CRC64;
     MDSRPMEDYL IYLKVEKGLA PNTVESYQRD IRHYVDYLSE QGIKSWEEID RYVLLSFFSE
     ERQSDKSDNT IIRQFSSLRK FHQFLKQEGV TPEDPMLYVK TPKKAETLPK IISMNEIDRL
     LETPDTAKPL GIRDRAMLEV LYATGLRITE LIELTTEDIH LSMKLIQIVG KGNKERLIPI
     GEMGCKWLDY YMESARPFLL KKAKKETSVI FLNSRGAPLS RQGVWKKIRQ LKQEAGIRAS
     ITPHTLRHSF ATHLLENGAD LRVVQELLGH ANVSTTQIYT HITKHRLKDI YGKYHPRA
//
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