LACB2_BOVIN
ID LACB2_BOVIN Reviewed; 288 AA.
AC Q1LZ83;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-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 -!- SUBUNIT: Monomer. {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; BC116149; AAI16150.1; -; mRNA.
DR RefSeq; NP_001069513.1; NM_001076045.2.
DR AlphaFoldDB; Q1LZ83; -.
DR SMR; Q1LZ83; -.
DR STRING; 9913.ENSBTAP00000002364; -.
DR PaxDb; Q1LZ83; -.
DR PRIDE; Q1LZ83; -.
DR Ensembl; ENSBTAT00000002364; ENSBTAP00000002364; ENSBTAG00000001808.
DR GeneID; 535021; -.
DR KEGG; bta:535021; -.
DR CTD; 51110; -.
DR VEuPathDB; HostDB:ENSBTAG00000001808; -.
DR VGNC; VGNC:30765; LACTB2.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00390000001710; -.
DR HOGENOM; CLU_048478_1_2_1; -.
DR InParanoid; Q1LZ83; -.
DR OMA; EFYLAHR; -.
DR OrthoDB; 576967at2759; -.
DR TreeFam; TF314297; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000001808; Expressed in spermatocyte and 104 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 Acetylation; Endonuclease; Hydrolase; Metal-binding; Mitochondrion;
KW Nuclease; Phosphoprotein; Reference proteome; RNA-binding; Zinc.
FT CHAIN 1..288
FT /note="Endoribonuclease LACTB2"
FT /id="PRO_0000315742"
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 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q53H82"
FT BINDING 118
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"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR3"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR3"
FT MOD_RES 273
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR3"
FT MOD_RES 282
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR3"
SQ SEQUENCE 288 AA; 32683 MW; 469B821FE0170E28 CRC64;
MAATLQRIER LSSRVIRVLG CNPGPMTLQG TNTYLVGTGP RRILIDTGEP SIPEYISCLK
QALTEFNTAI QEIIVTHWHR DHTGGIGDIC KSINNDTTYC VKKLPRNPER KEIIGNGEQQ
YVYVKDGDII KTEGATLRVV YTPGHTDDHM ALVLEEENAL FSGDCILGEG TTVFEDLYDY
MNSLKELLKI KAKVIYPGHG PVIHNAEAKI LQYISHRNIR EQQILTVFHE NFEKSFTAME
LVKSIYKDTP EHLHKMAQHN VLLHLKKLEK EGKIVSNTDP EKKWKAHL
