ID RNJ_SYNY3 Reviewed; 640 AA. AC P54123; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 142. DE RecName: Full=Ribonuclease J {ECO:0000255|HAMAP-Rule:MF_01491}; DE Short=RNase J {ECO:0000255|HAMAP-Rule:MF_01491}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01491}; GN Name=rnj {ECO:0000255|HAMAP-Rule:MF_01491}; OrderedLocusNames=slr0551; OS Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Merismopediaceae; Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: An RNase that has 5'-3' exonuclease and possibly CC endoonuclease activity. Involved in maturation of rRNA and in some CC organisms also mRNA maturation and/or decay (By similarity). CC {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01491}; CC Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) CC or Mg(2+) is physiologically important. {ECO:0000255|HAMAP- CC Rule:MF_01491}; CC -!- SUBUNIT: Homodimer, may be a subunit of the RNA degradosome. CC {ECO:0000255|HAMAP-Rule:MF_01491}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01491}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000022; BAA10871.1; -; Genomic_DNA. DR PIR; S76024; S76024. DR AlphaFoldDB; P54123; -. DR SMR; P54123; -. DR FunCoup; P54123; 254. DR IntAct; P54123; 4. DR STRING; 1148.gene:10500377; -. DR PaxDb; 1148-gene:10500377; -. DR EnsemblBacteria; BAA10871; BAA10871; BAA10871. DR KEGG; syn:slr0551; -. DR eggNOG; COG0595; Bacteria. DR InParanoid; P54123; -. DR PhylomeDB; P54123; -. DR Proteomes; UP000001425; 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; IBA:GO_Central. DR GO; GO:0004532; F:RNA exonuclease activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006397; P:mRNA processing; IBA:GO_Central. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. 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; IPR055132; RNase_J_b_CASP. 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; PF22505; RNase_J_b_CASP; 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; Endonuclease; Exonuclease; Hydrolase; Metal-binding; Nuclease; KW Reference proteome; RNA-binding; rRNA processing; Zinc. FT CHAIN 1..640 FT /note="Ribonuclease J" FT /id="PRO_0000215273" FT REGION 578..640 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 598..610 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491" FT BINDING 77 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491" FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491" FT BINDING 80 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491" FT BINDING 167 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491" FT BINDING 167 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491" FT BINDING 368..372 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491" FT BINDING 394 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01491" SQ SEQUENCE 640 AA; 70427 MW; F4D1CC23EA656E6D CRC64; MAKNTQTQAL KILPLGGLHE IGKNTCVFEY DDEILLLDAG LAFPTDDMHG VNVVLPDMTY LRENREKIKG MVVTHGHEDH IGGIAYHLKQ FDIPIIYGPR LAMALLRDKL EEAGMLERTN LQTVSPREMV RLGKSFVVEF IRNTHSIADS YCLAIHTPLG VVMHSGDFKI DHTPIDGEFF DLQKVAEYGE KGVLCLLSDS TNAEVPGITP SEASVIPNLD RVFSQAEGRL MVTTFASSVH RVNIILSLAQ KHQRKVAVVG RSMLNVIAHA RKLGYIKCPD NLFVPLKAAR NLPDQQQLIL TTGSQGEPLA AMTRISNGEH PQIKIRQGDT VVFSANPIPG NTIAVVNTID RLMMQGANVI YGKHQGIHVS GHASQEEHKM LLALTRPKFF VPVHGEHRML VKHSQMAQAQ GIPSENIVIV NNGDVIELTG DRIRVAGQVP SGIELVDQAG IVHESTMAER QQMAEDGLVT VAAALSKTGT LLAYPEVHCR GVVMTIQPKL LEELIVRTIE NFLTERWSEF THGSNGSTEV SWNALQKELE SSLQRLIKRE LQSSPMVLLM LQTDTPIELD QVPQNVSTVS ATSATPAPRK KVVLTKTPEP KVKAKPEKKV VTTAEPSAQP VSTTKVYRRS RKRSTTSVSS //