ID   LACB2_XENLA             Reviewed;         287 AA.
AC   Q5XGR8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Endoribonuclease LACTB2 {ECO:0000250|UniProtKB:Q53H82};
DE   AltName: Full=Beta-lactamase-like protein 2;
DE            EC=3.1.27.- {ECO:0000250|UniProtKB:Q53H82};
GN   Name=lactb2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoribonuclease; cleaves preferentially 3' to purine-
CC       pyrimidine dinucleotide motifs in single-stranded RNA. The cleavage
CC       product contains a free 3' -OH group. Has no activity with double-
CC       stranded RNA or DNA. Required for normal mitochondrial function and
CC       cell viability. {ECO:0000250|UniProtKB:Q53H82}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q53H82};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q53H82};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q53H82}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family. {ECO:0000305}.
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; BC084364; AAH84364.1; -; mRNA.
DR   RefSeq; NP_001088412.1; NM_001094943.1.
DR   AlphaFoldDB; Q5XGR8; -.
DR   SMR; Q5XGR8; -.
DR   MaxQB; Q5XGR8; -.
DR   PRIDE; Q5XGR8; -.
DR   DNASU; 495268; -.
DR   GeneID; 495268; -.
DR   KEGG; xla:495268; -.
DR   CTD; 495268; -.
DR   Xenbase; XB-GENE-954715; lactb2.L.
DR   OrthoDB; 576967at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 495268; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; ISS:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR041516; LACTB2_WH.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF17778; BLACT_WH; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   2: Evidence at transcript level;
KW   Endonuclease; Hydrolase; Metal-binding; Mitochondrion; Nuclease;
KW   Reference proteome; RNA-binding; Zinc.
FT   CHAIN           1..287
FT                   /note="Endoribonuclease LACTB2"
FT                   /id="PRO_0000315747"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
SQ   SEQUENCE   287 AA;  32419 MW;  6AF970C5B47E4195 CRC64;
     MSLSVLPRLE QLSSRVVRVL GCNPGPMTLQ GTNTYLVGTG SRRILIDTGE PAVPEYISCL
     KQALIEFNTS IQEIIVTHWH VDHVGGIADI SRDIMKGCNF SINKLPRNPH QEEVIADHKY
     NYLKDGDIIT TEGATLRVLY TPGHTDDHMA LELLEENAIF SGDCILGEGT AVFEDLYDYM
     KSLEKLLEMK ADKIYPGHGP VVLGARAKIQ EYISHRHARE QQILQALQEN RGKSFTSMDL
     VKIVYKDTPE YLHKAAEFNL THHLQKLKKE GKISEEQSPT VRWRSNL