ID YBEY_BRUME Reviewed; 168 AA. AC P67132; Q8FXU1; Q8YEA4; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 94. 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}; GN OrderedLocusNames=BMEI1974; OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=224914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16M / ATCC 23456 / NCTC 10094; RX PubMed=11756688; DOI=10.1073/pnas.221575398; RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., RA Haselkorn R., Kyrpides N.C., Overbeek R.; RT "The genome sequence of the facultative intracellular pathogen Brucella RT melitensis."; RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(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; Evidence={ECO:0000255|HAMAP- CC 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}. 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; AE008917; AAL53155.1; -; Genomic_DNA. DR PIR; AH3498; AH3498. DR AlphaFoldDB; P67132; -. DR SMR; P67132; -. DR KEGG; bme:BMEI1974; -. DR eggNOG; COG0319; Bacteria. DR PhylomeDB; P67132; -. DR Proteomes; UP000000419; Chromosome I. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule. 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; Metalloproteases ('zincins'), catalytic domain; 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 NCBIfam; TIGR00043; rRNA maturation RNase YbeY; 1. DR PANTHER; PTHR46986; ENDORIBONUCLEASE YBEY, CHLOROPLASTIC; 1. DR PANTHER; PTHR46986:SF1; YBEY METALLOENDORIBONUCLEASE; 1. DR Pfam; PF02130; YbeY; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS01306; UPF0054; 1. PE 3: Inferred from homology; KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease; KW Ribosome biogenesis; rRNA processing; Zinc. FT CHAIN 1..168 FT /note="Endoribonuclease YbeY" FT /id="PRO_0000102423" FT BINDING 122 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009" FT BINDING 126 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009" SQ SEQUENCE 168 AA; 18423 MW; BC6B2B7F0F074795 CRC64; MSDNAIHIDI MIEAGNWPDE ASLESLVSKS VAAAWNNLGL KSATSELSVV FTDDASIQLL NGEWRGKDKP TNVLSFPAFP VKAGSQPGPM LGDIVIARET VEREAKEEGK PIENHLSHLV VHGFLHLLGY DHETDEEAEV MEAREREILH ALAIPDPYAV SDEDINND //