ID   RECU_UREPA              Reviewed;         170 AA.
AC   Q9PQJ4;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Holliday junction resolvase RecU;
DE            EC=3.1.21.10 {ECO:0000255|HAMAP-Rule:MF_00130};
DE   AltName: Full=Recombination protein U homolog;
GN   Name=recU; OrderedLocusNames=UU297;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
CC   -!- FUNCTION: Endonuclease that resolves Holliday junction intermediates in
CC       genetic recombination. Cleaves mobile four-strand junctions by
CC       introducing symmetrical nicks in paired strands. Promotes annealing of
CC       linear ssDNA with homologous dsDNA. Required for DNA repair, homologous
CC       recombination and chromosome segregation (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage at a junction such as a reciprocal
CC         single-stranded crossover between two homologous DNA duplexes
CC         (Holliday junction).; EC=3.1.21.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00130};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RecU family. {ECO:0000305}.
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DR   EMBL; AF222894; AAF30706.1; -; Genomic_DNA.
DR   RefSeq; WP_010891726.1; NC_002162.1.
DR   AlphaFoldDB; Q9PQJ4; -.
DR   SMR; Q9PQJ4; -.
DR   STRING; 273119.UU297; -.
DR   EnsemblBacteria; AAF30706; AAF30706; UU297.
DR   GeneID; 29672508; -.
DR   KEGG; uur:UU297; -.
DR   PATRIC; fig|273119.6.peg.309; -.
DR   eggNOG; COG3331; Bacteria.
DR   HOGENOM; CLU_096340_2_0_14; -.
DR   OMA; TDYNGIY; -.
DR   Proteomes; UP000000423; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1350.10; -; 1.
DR   HAMAP; MF_00130; RecU; 1.
DR   InterPro; IPR004612; Resolv_RecU.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR   Pfam; PF03838; RecU; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..170
FT                   /note="Holliday junction resolvase RecU"
FT                   /id="PRO_0000212320"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            72
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   170 AA;  20527 MW;  892315A8C36933DD CRC64;
     MNNKNNGMHL EVLINKSISL FNLQYQAFFK KRCVDIIIKN IDNSYVQGKI KQKSETDYYG
     FYKGDYFDFE AKQTNKNSFL IKQIQPHQLA HLYLIHKNSG FSFLIICFIN YNLYFIITFQ
     QLINYYQKTK RKSIPFQWFK DQCIELEIIF PGVINFKKMI NDLKLKYYDD