YBEY_SYNJA
ID YBEY_SYNJA Reviewed; 163 AA.
AC Q2JU40;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 78.
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=CYA_1624;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC99784.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000239; ABC99784.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041438372.1; NC_007775.1.
DR AlphaFoldDB; Q2JU40; -.
DR SMR; Q2JU40; -.
DR STRING; 321327.CYA_1624; -.
DR EnsemblBacteria; ABC99784; ABC99784; CYA_1624.
DR KEGG; cya:CYA_1624; -.
DR eggNOG; COG0319; Bacteria.
DR HOGENOM; CLU_106710_3_1_3; -.
DR OrthoDB; 1830156at2; -.
DR Proteomes; UP000008818; 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 Ribosome biogenesis; rRNA processing; Zinc.
FT CHAIN 1..163
FT /note="Endoribonuclease YbeY"
FT /id="PRO_0000284336"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
SQ SEQUENCE 163 AA; 18526 MW; FE7FFBE98DD75F24 CRC64;
MEGFLDLYLE LNVPSPVEEA TWHRWFEVWL RELGVTDPCE LSLCLTSDEH IRQLNREFRH
IDAPTDVLAF AAEETSTPVE LQKITGVRLL GDIVISVPTA CAQAKAQGQR LSRELAWLAS
HGLLHLLGWD HPDELSLQRM LQQQHHLLAA IQEDLEVTHG QQP
