ID W5ITC3_PSEUO Unreviewed; 153 AA.
AC W5ITC3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=PM1_0205015 {ECO:0000313|EMBL:ETM65548.1};
OS Pseudomonas sp. (strain M1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=95619 {ECO:0000313|EMBL:ETM65548.1};
RN [1] {ECO:0000313|EMBL:ETM65548.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM65548.1};
RX PubMed=10388678;
RA Iurescia S., Marconi A.M., Tofani D., Gambacorta A., Paterno A.,
RA Devirgiliis C., van der Werf M.J., Zennaro E.;
RT "Identification and sequencing of beta-myrcene catabolism genes from
RT Pseudomonas sp. strain M1.";
RL Appl. Environ. Microbiol. 65:2871-2876(1999).
RN [2] {ECO:0000313|EMBL:ETM65548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM65548.1};
RA Soares-Castro P.M., Santos P.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETM65548.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM65548.1};
RX PubMed=23405299;
RA Soares-Castro P., Santos P.M.;
RT "Towards the Description of the Genome Catalogue of Pseudomonas sp. Strain
RT M1.";
RL Genome Announc. 1:E00146-E00112(2013).
RN [4] {ECO:0000313|EMBL:ETM65548.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM65548.1};
RA Soares-Castro P., Santos P.M.;
RT "Decyphering the genome repertoire of Pseudomonas sp. M1 towards myrcene
RT biotransformation.";
RL Submitted (DEC-2013) 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}.
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:ETM65548.1}.
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; ANIR02000002; ETM65548.1; -; Genomic_DNA.
DR RefSeq; WP_009617340.1; NZ_CP094343.1.
DR AlphaFoldDB; W5ITC3; -.
DR eggNOG; COG0319; Bacteria.
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}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_00009};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00009}.
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="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 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
SQ SEQUENCE 153 AA; 17186 MW; 64F90A48C9D992E5 CRC64;
MLELDLQVAS QAADLPAEAQ LRQWCELALR QRQADSELTI RLVDEAEGRE LNRTWRHKDY
ATNVLSFPAD VPDELLDIPL LGDLVICVPV VEREAAEQGK APAAHWAHLV IHGCLHLLGY
DHIEDAEAEE MEALERQLLA ELGYPDPYAA DEE
//
