LACB2_DANRE
ID LACB2_DANRE Reviewed; 289 AA.
AC Q6NYF0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
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; ORFNames=zgc:77065;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-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}.
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DR EMBL; BC066620; AAH66620.1; -; mRNA.
DR RefSeq; NP_998049.1; NM_212884.1.
DR AlphaFoldDB; Q6NYF0; -.
DR SMR; Q6NYF0; -.
DR STRING; 7955.ENSDARP00000024616; -.
DR PaxDb; Q6NYF0; -.
DR GeneID; 405820; -.
DR KEGG; dre:405820; -.
DR CTD; 51110; -.
DR ZFIN; ZDB-GENE-040426-2257; lactb2.
DR eggNOG; KOG0813; Eukaryota.
DR InParanoid; Q6NYF0; -.
DR OrthoDB; 576967at2759; -.
DR PhylomeDB; Q6NYF0; -.
DR PRO; PR:Q6NYF0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0048856; P:anatomical structure development; IEA:UniProt.
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_0000315746"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
SQ SEQUENCE 289 AA; 32404 MW; B98DCE17A33E5E50 CRC64;
MSAVIPRIEQ LSARVVRVLG CNPGPMTLQG TNTYLVGTGR RRVLIDAGER AVPEYIVSLR
EALKQHDTSI QHIIVTHWHH DHTGGVQDIL AHFNTDAELR VSKLPRCPPQ EEIIGDDKKK
YSYLNDGDVI QTEGATLRVL FTPGHTDDHM ALLLEEEQAV FSGDCILGEG TAVFEDLHDY
MKSLQKLLSI KADLIYPGHG PVVHDAGSKI HEYIIHRNAR EQQILNVLLE NSGTAFTSSE
LVKVVYKETP EHLHRAAEFN LLHHLRKLLK DGKICLAEGS DEKKWKSNL
