ID   LACB2_XENTR             Reviewed;         289 AA.
AC   Q0V9A9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 55.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) 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}.
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DR   EMBL; BC121666; AAI21667.1; -; mRNA.
DR   RefSeq; NP_001072425.1; NM_001078957.1.
DR   AlphaFoldDB; Q0V9A9; -.
DR   SMR; Q0V9A9; -.
DR   DNASU; 779879; -.
DR   GeneID; 779879; -.
DR   KEGG; xtr:779879; -.
DR   CTD; 51110; -.
DR   Xenbase; XB-GENE-954710; lactb2.
DR   InParanoid; Q0V9A9; -.
DR   OrthoDB; 576967at2759; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
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..289
FT                   /note="Endoribonuclease LACTB2"
FT                   /id="PRO_0000315748"
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         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H82"
SQ   SEQUENCE   289 AA;  32420 MW;  574D0A5EE958DC23 CRC64;
     MALSVLPRLE QLSARVVRVL GCNPGPMTLQ GTNTYLVGTG PRRILIDTGE PAVPEYISCL
     KQALTEFNTS IQEIIVTHWH VDHVGGIADI CTDIMNGCNF SVSKLPRNPH QEEVIGAVEH
     KYNYLKDGDI ITTEGATLRV LYTPGHTDDH MALELLEENA IFSGDCILGE GTAVFEDLYD
     YMKSLEKLLE MKADKIYPGH GPVVLGARAK IQEYISHRHA REQQILQALQ ENSGRSFTSM
     DLVKIVYKDT PEYLHKAAEF NLTHHLQKLK KEGKISEEQS PTVRWRSNL