ID A0A160N201_9GAMM Unreviewed; 154 AA.
AC A0A160N201;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Endoribonuclease YbeY {ECO:0000256|HAMAP-Rule:MF_00009};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00009};
GN Name=ybeY {ECO:0000256|HAMAP-Rule:MF_00009};
GN ORFNames=ATSB10_21000 {ECO:0000313|EMBL:AND69554.1};
OS Dyella thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=445710 {ECO:0000313|EMBL:AND69554.1, ECO:0000313|Proteomes:UP000077255};
RN [1] {ECO:0000313|EMBL:AND69554.1, ECO:0000313|Proteomes:UP000077255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATSB10 {ECO:0000313|EMBL:AND69554.1,
RC ECO:0000313|Proteomes:UP000077255};
RA Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y.,
RA Madhaiyan M.;
RT "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans
RT isolated from rhizosphere soil of sunflower (Helianthus annuus L.).";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00009}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00009};
CC Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00009};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00009}.
CC -!- SIMILARITY: Belongs to the endoribonuclease YbeY family.
CC {ECO:0000256|ARBA:ARBA00010875, ECO:0000256|HAMAP-Rule:MF_00009}.
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DR EMBL; CP014841; AND69554.1; -; Genomic_DNA.
DR RefSeq; WP_063672547.1; NZ_CP014841.1.
DR AlphaFoldDB; A0A160N201; -.
DR STRING; 445710.ATSB10_21000; -.
DR KEGG; dtx:ATSB10_21000; -.
DR PATRIC; fig|445710.3.peg.2098; -.
DR OrthoDB; 9807740at2; -.
DR Proteomes; UP000077255; Chromosome.
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 {ECO:0000256|HAMAP-Rule:MF_00009};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00009};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00009};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00009};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00009};
KW Reference proteome {ECO:0000313|Proteomes:UP000077255};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00009}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_00009};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00009}.
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
SQ SEQUENCE 154 AA; 16633 MW; 1F5F7E82602BEAED CRC64;
MSANTVVHVG YAVPRAGVPS AASFRQWVEA ALRGAKRRRA TELSIRLVDA DEGRALNRDY
RGKDYATNVL SFEADLPPEL KLPLIGDIVI CAPVVAREAA EQGKTPRDHW AHLTVHGVLH
LLGHDHIEEA EAAAMEALET RILAGLGIAD PYAG
//
