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Database: UniProt
Entry: D4N003_ANAHA
LinkDB: D4N003_ANAHA
Original site: D4N003_ANAHA 
ID   D4N003_ANAHA            Unreviewed;       170 AA.
AC   D4N003;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=CL2_12210 {ECO:0000313|EMBL:CBL38198.1}, ERS852475_00097
GN   {ECO:0000313|EMBL:CUN43456.1};
OS   Anaerostipes hadrus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL38198.1, ECO:0000313|Proteomes:UP000008960};
RN   [1] {ECO:0000313|EMBL:CBL38198.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38198.1,
RC   ECO:0000313|Proteomes:UP000008960};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SSC/2.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL38198.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38198.1,
RC   ECO:0000313|Proteomes:UP000008960};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CUN43456.1, ECO:0000313|Proteomes:UP000095611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5834860 {ECO:0000313|EMBL:CUN43456.1,
RC   ECO:0000313|Proteomes:UP000095611};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) 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; FP929061; CBL38198.1; -; Genomic_DNA.
DR   EMBL; CYZM01000001; CUN43456.1; -; Genomic_DNA.
DR   RefSeq; WP_008391323.1; NZ_JAAIQS010000014.1.
DR   AlphaFoldDB; D4N003; -.
DR   STRING; 649756.ERS852387_01893; -.
DR   GeneID; 15231289; -.
DR   KEGG; bprl:CL2_12210; -.
DR   PATRIC; fig|245018.3.peg.1538; -.
DR   Proteomes; UP000008960; Chromosome.
DR   Proteomes; UP000095611; Unassembled WGS sequence.
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   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_00009};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_00009};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00009}.
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   170 AA;  20061 MW;  D75585B7C5EC5542 CRC64;
     MSIIIENEYE GEINIPYEKI AHEVIEAAID YVDCPYECEV NLMLTNNETI HAINKEQREI
     DRPTDVLSFP MAEYEEPADF SKIEEDPMAF DPESGEFLLG DIVISMDKVW EQAENYGHSR
     EREYAFLIAH SMLHLFGYDH MEEEERKDME KRQEEILTKT KYTRDERGLV
//
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