ID A0A0D8ZMM8_9CYAN Unreviewed; 588 AA.
AC A0A0D8ZMM8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=UH38_22415 {ECO:0000313|EMBL:KJH69684.1};
OS Aliterella atlantica CENA595.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Aliterellaceae; Aliterella.
OX NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH69684.1, ECO:0000313|Proteomes:UP000032452};
RN [1] {ECO:0000313|EMBL:KJH69684.1, ECO:0000313|Proteomes:UP000032452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA595 {ECO:0000313|EMBL:KJH69684.1,
RC ECO:0000313|Proteomes:UP000032452};
RA Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA Fiore M.F.;
RT "Draft genome of a novel marine cyanobacterium (Chroococcales) isolated
RT from South Atlantic Ocean.";
RL Submitted (FEB-2015) 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:KJH69684.1}.
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DR EMBL; JYON01000036; KJH69684.1; -; Genomic_DNA.
DR RefSeq; WP_045056934.1; NZ_JYON01000036.1.
DR AlphaFoldDB; A0A0D8ZMM8; -.
DR STRING; 1618023.UH38_22415; -.
DR PATRIC; fig|1618023.3.peg.3000; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000032452; 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|HAMAP-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 Reference proteome {ECO:0000313|Proteomes:UP000032452};
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 20..217
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 366..370
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 588 AA; 65242 MW; 588FC5F6F2B6DDF3 CRC64;
MTKSSPTIKI IPLGGLHEIG KNTCVFECED EIILLDAGLA FPTDGMHGVN IVLPDMTYLR
ENRHKIKGMI VTHGHEDHIG GIAFHLKQLE IPVIYGPRLA MAMLEGKLEE AGVRDRTELR
SVRPRDMVRL GSHFVVEFIR NTHSIADSFT VALHTPAGII IHTGDFKFDH TPVDGEHFDI
QRLAEHGEKG VLCLISDSTN SEIPGHTPSE RSVYPNLARV FSEAKGRLLV TTFASSVHRI
NMILELAKLQ NRVVGVVGRS MLNLIAHARN LGYIKCEDNL LQPLQAIRNL PDEKVLILTT
GSQGEPMSAM TRISKGEHQH IKIRPGDTVV FSANPIPGNT IAVVNTIDRL MMQGANVIYG
REKGLHVSGH GCQEDQKLMI ALTKPKFFLP VHGEHRMLIK HSQTAQSTGI PAENMVIIQN
GDVVEVSPEA IRVAGKVPSG VELVDMSRTG IVSDRVLKER QQMAEEGTIV IAAAVDWQGK
LMMKPEIHVR GVVTSIERSL LQKWVQERME QVLSDRWSSF AQFVNGEPVE VDWAGVQVQL
ERELQRAIRR ELQCQPSIIL LMQTPDEPAA KAVDGRRRRR TTAQVAAS
//
