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Database: UniProt
Entry: A0A2T4ZAL6_9BACL
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ID   A0A2T4ZAL6_9BACL        Unreviewed;       559 AA.
AC   A0A2T4ZAL6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803};
DE            Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803};
GN   Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN   ORFNames=C8J48_1543 {ECO:0000313|EMBL:PTM58944.1};
OS   Desmospora activa DSM 45169.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Desmospora.
OX   NCBI_TaxID=1121389 {ECO:0000313|EMBL:PTM58944.1, ECO:0000313|Proteomes:UP000241639};
RN   [1] {ECO:0000313|EMBL:PTM58944.1, ECO:0000313|Proteomes:UP000241639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45169 {ECO:0000313|EMBL:PTM58944.1,
RC   ECO:0000313|Proteomes:UP000241639};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (APR-2018) 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR004803};
CC       Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or
CC       Mg(2+) is physiologically important. {ECO:0000256|PIRNR:PIRNR004803};
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       ECO:0000256|PIRNR:PIRNR004803}.
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       ECO:0000256|PIRNR:PIRNR004803}.
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:PTM58944.1}.
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DR   EMBL; PZZP01000001; PTM58944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4ZAL6; -.
DR   OrthoDB; 9758375at2; -.
DR   Proteomes; UP000241639; 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:SF4; RIBONUCLEASE J2; 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   ECO:0000256|PIRNR:PIRNR004803};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01491};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241639};
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..217
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   BINDING         368..372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT                   ECO:0000256|PIRSR:PIRSR004803-2"
SQ   SEQUENCE   559 AA;  61629 MW;  F3C784AAC8AD8D08 CRC64;
     MTKNNSRSKL TIFALGGLDE IGKNMYVVRY GDDIVVIDSG LMFPEEEMLG IDVVIPDVTY
     LVENQDKVRG ILLTHGHEDH IGGLPYILKQ LNVPIFGTKL TMGLVEHKLR EAHLLNQTKR
     VLVNNRSEIK LGSIKATFFR TNHSIPDSVG VCLETPEGNV VHTGDFKFDM TPVNGKEADI
     HKMAEIGQKG VLCLLSDSTN AERPGFTGSE REVGEAIENL FRKSKQRVIV ATFASNIHRI
     QQVVDATCKY NRKLAVIGRS MVNVVNIGME LGYLHVPPDL LIDPDDINRL PAHKVTVMST
     GSQGEPMSAL TRMAHGSHRK IEILPGDTVI LAATPIPGNE KAVARTVNQL FRVGADVFYS
     NNTQQGVHVS GHGSQEDLKL MLNLMKPQFF IPIHGEHRML RAHGQLAESI GVPSENIFVC
     DNGDAVEISG GKARYGTKIT TGNVLIDGLG VGDVGNIVLR DRKLLSQDGI LVVVVTLSKN
     NGKVLSGPDI ISRGFVYVRE SEKLLEEANR IVTQTMEKCA NERVSEWASL KTSIRDALGR
     YLYDQTRRRP MILPIIMEV
//
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