ID A0A1G2D3Q7_9BACT Unreviewed; 573 AA.
AC A0A1G2D3Q7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=A3D65_02755 {ECO:0000313|EMBL:OGZ08265.1};
OS Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_02_FULL_50_13.
OC Bacteria; Candidatus Lloydbacteria.
OX NCBI_TaxID=1798661 {ECO:0000313|EMBL:OGZ08265.1, ECO:0000313|Proteomes:UP000177996};
RN [1] {ECO:0000313|EMBL:OGZ08265.1, ECO:0000313|Proteomes:UP000177996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:OGZ08265.1}.
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DR EMBL; MHLL01000039; OGZ08265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2D3Q7; -.
DR STRING; 1798661.A3D65_02755; -.
DR Proteomes; UP000177996; 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 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.
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 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 32..228
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 377..381
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 573 AA; 64177 MW; 4D4DDCEBCA93DCC3 CRC64;
MRRHIAEEKA NIPELVKGDV RIVILGGVEE IGRNMAAIEF GNDIIIVDCG FMFKDEDAPG
VDYILPNTQY LEERKERIRG VFITHGHLDH IGGLPYILPL IGNPPVYARN LTALLIQKRQ
DEFPELPPID LKVVETEDRI SFTDISVRFF KVTHTIPDSM GIMIETPYGV IVHTGDLKLD
HLAGVATDIE KKAYSKFDKE KVLLLMADST NCQKPGFSIP EPTVHVTVEE LIKNSRGRVI
VATFSSLLER IIKIIEFADK HGRKIVVDGR SMKTNIELAQ KAGLFTYKKG TVIGIEEMDS
YPPEKIVMLV TGAQGDPFAV LMRVATKVHK SLKIQDGDTV LFSSSVIPGN ERAVQKLKDL
LSRQGAKIVH YETSDVHSSG HAYHDELLWL IGHIHPKFFI PLHGYHYMLR SHVEIAQATG
LPRENTLIAD NGSIVEIREG GEKIVKLSVS APKEMIMVDG FAIGNLQEVV MRDRKMLAED
GIVVLVATVD MHTGKLMKSP DIIARGFVYV RESQELLNQA RLIIKKTIED ECGRGMKGVN
FEYLKEDVRD QVGKFLFQKT QKQPMVIPVL LGI
//
