位置:首页 > 蛋白库 > RECU_BACVZ
RECU_BACVZ
ID   RECU_BACVZ              Reviewed;         202 AA.
AC   A7Z5Y2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Holliday junction resolvase RecU {ECO:0000255|HAMAP-Rule:MF_00130};
DE            EC=3.1.21.10 {ECO:0000255|HAMAP-Rule:MF_00130};
DE   AltName: Full=Recombination protein U homolog {ECO:0000255|HAMAP-Rule:MF_00130};
GN   Name=recU {ECO:0000255|HAMAP-Rule:MF_00130}; OrderedLocusNames=RBAM_020460;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00130}.
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;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00130};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00130};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00130}.
CC   -!- SIMILARITY: Belongs to the RecU family. {ECO:0000255|HAMAP-
CC       Rule:MF_00130}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000560; ABS74408.1; -; Genomic_DNA.
DR   RefSeq; WP_012117837.1; NC_009725.2.
DR   AlphaFoldDB; A7Z5Y2; -.
DR   SMR; A7Z5Y2; -.
DR   STRING; 326423.RBAM_020460; -.
DR   EnsemblBacteria; ABS74408; ABS74408; RBAM_020460.
DR   KEGG; bay:RBAM_020460; -.
DR   HOGENOM; CLU_096340_0_0_9; -.
DR   OMA; TDYNGIY; -.
DR   Proteomes; UP000001120; 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   PIRSF; PIRSF037785; RecU; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR00648; recU; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA recombination; DNA repair; Endonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease.
FT   CHAIN           1..202
FT                   /note="Holliday junction resolvase RecU"
FT                   /id="PRO_1000016714"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   BINDING         101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
FT   SITE            103
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00130"
SQ   SEQUENCE   202 AA;  23667 MW;  219ED1712F6072A0 CRC64;
     MIRYPNGKTF QPNKTVSSQN SQKRSHSYSN RGMTLEDDLN ETNKYYLANQ IAVIHKKPTP
     VQIVNVHYPK RSAAVIKEAY FKQSSTTDYN GIYKGRYIDF EAKETKNKTA FPLQNFHDHQ
     IEHMKQVVRQ DGICFVIISA FGKVYFLEAD KLFVFWERKE NNGRKSIRKD ELEDASFPIS
     LGYSPRIDYI SIIEQLYFSQ EQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024