ID A0A117M4A9_9BACT Unreviewed; 560 AA.
AC A0A117M4A9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 08-NOV-2023, entry version 26.
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=XD98_0302 {ECO:0000313|EMBL:KUK83605.1};
OS Microgenomates bacterium 39_6.
OC Bacteria; Candidatus Microgenomates.
OX NCBI_TaxID=1641391 {ECO:0000313|EMBL:KUK83605.1, ECO:0000313|Proteomes:UP000053541};
RN [1] {ECO:0000313|Proteomes:UP000053541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK83605.1}.
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DR EMBL; LGGT01000035; KUK83605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117M4A9; -.
DR PATRIC; fig|1641391.3.peg.280; -.
DR Proteomes; UP000053541; 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; 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:SF1; RIBONUCLEASE J; 1.
DR Pfam; PF12706; Lactamase_B_2; 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01491};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01491};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01491}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01491};
KW Nuclease {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}.
FT DOMAIN 25..219
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 369..373
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 560 AA; 62503 MW; 6EA27B0FB0D33223 CRC64;
MNKETKNNQT DKLKIVSLGG FGLVTKNMFI YETPKDILIV DCGIGFPDEE MLGVDLVIPD
ISYLKNRKDK IRGIIISHGH EDHFGALPFL LPQLPKVPIF ASKLALAIAE RKLKENRIKA
DLRLIDRKRT LKLGDFEIDL IQVTHSVPEA QHMFIKTPHG NIYHGSDFKF DWTPIDKTKI
EVEKMVKASE RGVDLMLSDC LRSEREGYTD SEQALIEIFE REIAKAKGRF IVTTMSSNIS
RLKTAIDVSR ASGRKIALVG RSIVEIVKIG RRLGYLNLPK EDEINLRKVN NYPDEKVTLL
VAGSQAQSGS SLDRIASQAH DNIRIKPGDF VVFSTDYIPG NESSIQTVID LLMRQGAEVS
YMDISEDLHV SGHGARGDLS LLINLVKPKF LLPIGGGFRQ MKQYSLLAQR IGYQEDKILL
PSSGDVIEVD QGRASITGRF EARDVMVDGL GVGDVGNVVL RDREILSQEG VVSAVVMLDK
NKMQTIKEPE VLSRGFVYGQ IKDGKEILSL AQKEISRIVN GARKGMSTRD LKVAIQDSLE
KFFYSTTGRR PMVLLTIIEA
//
