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YBEY_BRADU
ID   YBEY_BRADU              Reviewed;         183 AA.
AC   Q89W99;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Endoribonuclease YbeY {ECO:0000255|HAMAP-Rule:MF_00009};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00009};
GN   Name=ybeY {ECO:0000255|HAMAP-Rule:MF_00009}; OrderedLocusNames=bll0793;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Single strand-specific metallo-endoribonuclease involved in
CC       late-stage 70S ribosome quality control and in maturation of the 3'
CC       terminus of the 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00009}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00009};
CC       Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00009};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00009}.
CC   -!- SIMILARITY: Belongs to the endoribonuclease YbeY family.
CC       {ECO:0000255|HAMAP-Rule:MF_00009}.
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DR   EMBL; BA000040; BAC46058.1; -; Genomic_DNA.
DR   RefSeq; NP_767433.1; NC_004463.1.
DR   AlphaFoldDB; Q89W99; -.
DR   SMR; Q89W99; -.
DR   STRING; 224911.27349042; -.
DR   EnsemblBacteria; BAC46058; BAC46058; BAC46058.
DR   KEGG; bja:bll0793; -.
DR   PATRIC; fig|224911.5.peg.817; -.
DR   eggNOG; COG0319; Bacteria.
DR   HOGENOM; CLU_106710_0_0_5; -.
DR   InParanoid; Q89W99; -.
DR   OMA; RMRIHPL; -.
DR   PhylomeDB; Q89W99; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.390.30; -; 1.
DR   HAMAP; MF_00009; Endoribonucl_YbeY; 1.
DR   InterPro; IPR023091; MetalPrtase_cat_dom_sf_prd.
DR   InterPro; IPR002036; YbeY.
DR   InterPro; IPR020549; YbeY_CS.
DR   PANTHER; PTHR46986; PTHR46986; 1.
DR   Pfam; PF02130; YbeY; 1.
DR   TIGRFAMs; TIGR00043; TIGR00043; 1.
DR   PROSITE; PS01306; UPF0054; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Reference proteome; Ribosome biogenesis; rRNA processing; Zinc.
FT   CHAIN           1..183
FT                   /note="Endoribonuclease YbeY"
FT                   /id="PRO_0000102422"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   183 AA;  20243 MW;  98471844CD98B689 CRC64;
     MGADASAFSF RTKTMSHPNL PMTEVLVVAD CWQREPDSEA VIQRAVAAAA ESVDEDVAEA
     EVAVMLTDDA GIRTLNSNWR GIDKPTNVLS FPALQPEGEW KEGDAPRMLG DIAIAYETMR
     READEEKKPF DHHLSHLAVH GFLHLIGYDH ENDDDAEEME ALETQILAHL GIPDPYADRP
     GTH
 
 
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