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Database: UniProt
Entry: A0A323V4I6_9ACTN
LinkDB: A0A323V4I6_9ACTN
Original site: A0A323V4I6_9ACTN 
ID   A0A323V4I6_9ACTN        Unreviewed;       304 AA.
AC   A0A323V4I6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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   ECO:0000313|EMBL:PZA19715.1};
GN   ORFNames=DMO24_19285 {ECO:0000313|EMBL:PZA19715.1}, FHX36_001065
GN   {ECO:0000313|EMBL:MBB3675330.1};
OS   Modestobacter versicolor.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=429133 {ECO:0000313|EMBL:PZA19715.1, ECO:0000313|Proteomes:UP000247602};
RN   [1] {ECO:0000313|EMBL:PZA19715.1, ECO:0000313|Proteomes:UP000247602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP153-2 {ECO:0000313|EMBL:PZA19715.1,
RC   ECO:0000313|Proteomes:UP000247602};
RA   Gundlapally S.R.;
RT   "Draft genome sequence of Modestobacter versicolor CP153-2.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB3675330.1, ECO:0000313|Proteomes:UP000580718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16678 {ECO:0000313|EMBL:MBB3675330.1,
RC   ECO:0000313|Proteomes:UP000580718};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2020) 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}.
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:PZA19715.1}.
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DR   EMBL; JACIBU010000001; MBB3675330.1; -; Genomic_DNA.
DR   EMBL; QKNV01000282; PZA19715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A323V4I6; -.
DR   OrthoDB; 9801717at2; -.
DR   Proteomes; UP000247602; Unassembled WGS sequence.
DR   Proteomes; UP000580718; 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:SF81; TYROSINE RECOMBINASE XERD; 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_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:UP000247602}.
FT   DOMAIN          1..87
FT                   /note="Core-binding (CB)"
FT                   /evidence="ECO:0000259|PROSITE:PS51900"
FT   DOMAIN          108..296
FT                   /note="Tyr recombinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51898"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        248
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        251
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
FT   ACT_SITE        283
FT                   /note="O-(3'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01807"
SQ   SEQUENCE   304 AA;  32129 MW;  BAE9142F43EA1D86 CRC64;
     MVSGYLDHLT VERGLAANTI ASYRRDLRRY AEFLAGAGVE GMGEVGESDV AAFLVALRSG
     DDDHPPLSAT SAARAVVAVR GLHRFALLDG LVGDDVAAEV KPPAPTRRLP KAIPVEQVEA
     LITAAGSLEG PRGLRDRALL ELLYGTGARI SEAVGLAVDD LDLGSAAVRL AGKGGKERVV
     PVGSYAVRAV EEYLVRARPA LAEKGRSGVR GGALFLNARG GPLSRQSAWS ILRDAAERAG
     IDAELSPHTL RHSFATHLLD GGADVRVVQE LLGHASVTTT QVYTLVTVER LREVYATSHP
     RALR
//
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