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Database: UniProt
Entry: I0R0S5_9MICO
LinkDB: I0R0S5_9MICO
Original site: I0R0S5_9MICO 
ID   I0R0S5_9MICO            Unreviewed;       152 AA.
AC   I0R0S5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=IMCC13023_10140 {ECO:0000313|EMBL:EIC91461.1};
OS   Candidatus Aquiluna sp. IMCC13023.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Aquiluna.
OX   NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC91461.1, ECO:0000313|Proteomes:UP000054510};
RN   [1] {ECO:0000313|Proteomes:UP000054510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX   PubMed=22689238; DOI=10.1128/JB.00586-12;
RA   Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT   "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT   member of the Actinobacteria isolated from an arctic fjord.";
RL   J. Bacteriol. 194:3550-3551(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIC91461.1}.
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DR   EMBL; AJKR01000003; EIC91461.1; -; Genomic_DNA.
DR   RefSeq; WP_007541980.1; NZ_AJKR01000003.1.
DR   AlphaFoldDB; I0R0S5; -.
DR   STRING; 1081644.IMCC13023_10140; -.
DR   PATRIC; fig|1081644.3.peg.1025; -.
DR   eggNOG; COG0319; Bacteria.
DR   OrthoDB; 9807740at2; -.
DR   Proteomes; UP000054510; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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}; Metalloprotease {ECO:0000313|EMBL:EIC91461.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00009};
KW   Protease {ECO:0000313|EMBL:EIC91461.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054510};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00009};
KW   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   152 AA;  17016 MW;  D99A8A40408AE60A CRC64;
     MSLEIANESE ITVDTERVLE LAYFVRGALK LHELVDLGIT FVDEGPMTDL HIKWMDEPGP
     TDVLSFPMDE LRPGTDRNSS PEGILGDIVV CPQVAIKQAK TAGHETINEI LLLVTHGMLH
     LVGFDHAEPE EEKEMFDLQK NLLADFYKLE TS
//
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