ID A0A249DCY7_LACRH Unreviewed; 560 AA.
AC A0A249DCY7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491};
DE Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491};
GN Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN ORFNames=BGK71_06175 {ECO:0000313|EMBL:ASX17010.1};
OS Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=47715 {ECO:0000313|EMBL:ASX17010.1, ECO:0000313|Proteomes:UP000215843};
RN [1] {ECO:0000313|EMBL:ASX17010.1, ECO:0000313|Proteomes:UP000215843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LR5 {ECO:0000313|EMBL:ASX17010.1,
RC ECO:0000313|Proteomes:UP000215843};
RA Nam Y.-D., Kang J., Chung W.-H.;
RT "Complete genome sequence of Lactobacillus rhamnosus LR5.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease
CC activity. Involved in maturation of rRNA and in some organisms also
CC mRNA maturation and/or decay. {ECO:0000256|HAMAP-Rule:MF_01491}.
CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome.
CC {ECO:0000256|HAMAP-Rule:MF_01491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01491}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. Bacterial RNase J
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01491}.
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DR EMBL; CP017063; ASX17010.1; -; Genomic_DNA.
DR RefSeq; WP_047677208.1; NZ_VRTQ01000001.1.
DR AlphaFoldDB; A0A249DCY7; -.
DR GeneID; 69831823; -.
DR Proteomes; UP000215843; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd07714; RNaseJ_MBL-fold; 1.
DR Gene3D; 3.10.20.580; -; 1.
DR Gene3D; 3.40.50.10710; Metallo-hydrolase/oxidoreductase; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR HAMAP; MF_01491; RNase_J_bact; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR InterPro; IPR004613; RNase_J.
DR InterPro; IPR042173; RNase_J_2.
DR InterPro; IPR030854; RNase_J_bac.
DR InterPro; IPR041636; RNase_J_C.
DR NCBIfam; TIGR00649; MG423; 1.
DR PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR PANTHER; PTHR43694:SF4; RIBONUCLEASE J 2; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01491};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_01491};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01491};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01491};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01491};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01491}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_01491};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 16..212
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 560 AA; 62223 MW; 674EE1F3AB5AC189 CRC64;
MTKINLVALG GVRENGKNMY AVEVDDQIFV CDFGLKYPDN ELLGIDVVIP DFSYLTENAD
RIAGIFLSHG HADAVGALPY FLVDHPVPVF GSELTIAMAK VFMQHDSKAK KFKDFHVIDE
KSVIDFGDVS VSFFKTTHSI PGSLGIDIET SEGQIVYTGD FKFDPSATPM YQTDWARLAQ
IGNKKVLALL SDSANAESPY PNANEHEIYD HIKETFEYQD GRIIVAGVAS NIQRIQQVIN
AAASLGRRVV LTGRDVEKVV KTAIRMGYIK LPDDDILAKT KELKGLAPEK TVILETGRMG
EPMKSLQRMA TSRHRLIHIH EGDLVFITTT IAHAMETMAA RTKDMIYRAG GDVKVLGDDI
HSSGHAYKND LQLMIDLLKP EYLVPVQGEY RLLAAHAEIA HEAGIPLANI FIVGMGDILR
YEKGQMNASG HVNAGNTMID GIGVGDIGNI VLRDRKMLAE DGIFIAVVTI DRKKKRVVSK
PKVTSRGFVY LKTSRDSLAE SGTLVTETVQ KNLDNKEFDW THLKQDVRDK LSRFLFEQTK
RRPVILPVIM EVNQNSAKRQ
//
