ID A0A1E5G910_9ENTE Unreviewed; 556 AA.
AC A0A1E5G910;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BCR25_11590 {ECO:0000313|EMBL:OEG09203.1};
OS Enterococcus termitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=332950 {ECO:0000313|EMBL:OEG09203.1, ECO:0000313|Proteomes:UP000095094};
RN [1] {ECO:0000313|EMBL:OEG09203.1, ECO:0000313|Proteomes:UP000095094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 8895 {ECO:0000313|EMBL:OEG09203.1,
RC ECO:0000313|Proteomes:UP000095094};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEG09203.1}.
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DR EMBL; MIJY01000045; OEG09203.1; -; Genomic_DNA.
DR RefSeq; WP_069664892.1; NZ_MIJY01000045.1.
DR AlphaFoldDB; A0A1E5G910; -.
DR PATRIC; fig|332950.4.peg.3189; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000095094; Unassembled WGS sequence.
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 InterPro; IPR001587; RNase_J_CS.
DR NCBIfam; TIGR00649; MG423; 1.
DR PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR PANTHER; PTHR43694:SF1; RIBONUCLEASE J; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 1.
DR PIRSF; PIRSF004803; RnjA; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS01292; UPF0036; 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 22..216
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 365..369
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 556 AA; 60581 MW; 66C26C5AFAE41C08 CRC64;
MKVNIKNNET GVFAIGGLGE IGKNTYGVQF QDEIIIIDAG IKFPEDDLLG IDYVIPDYSY
IVQNLHKVKA LVITHGHEDH IGGVPFLLRQ ANIPIYAGPL ALALITNKLD EHGLLRDAEL
HEINEDTVIR FRKTSISFFR TTHSIPDALG VVVKTPSGNI VATGDFKFDF TPVGEPANLH
RMAKLGEEGV LCLLSDSTNA EIPTFTKSEK TIGSSILKIF EKIEGRIIFA SFASNIFRLQ
QAADAAVKTG RKIAVFGRSM ENAIVNGEQL GYINVPKGTF VDASELNQLP AGETMILCTG
SQGEPMAALS RIANGTHRQI SVQPGDTVIF SSSPIPGNTT SVNRLINLLS EAGAEVIHGK
INNIHTSGHG GQEEQKLMLR LMKPKYFVPV HGEFRMLKIH ASLAQDVGVP AENCFIMENG
DVLALTADDA HIAGHFNAND VYVDGNGVGD IGNVVLRDRR ILSEEGLVLA VATVDIKNKE
ILAGPDILSR GFVYMRESGE MIHEGQRLLF NAIREALRDE NCTEAKLCDA ISAALQPFLF
EKTERHPMIL PMIMTS
//
