ID A0A3P0X9H1_9BACT Unreviewed; 553 AA.
AC A0A3P0X9H1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=D1Y84_11390 {ECO:0000313|EMBL:RRA48797.1};
OS Acidipila sp. EB88.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidipila.
OX NCBI_TaxID=2305226 {ECO:0000313|EMBL:RRA48797.1, ECO:0000313|Proteomes:UP000279598};
RN [1] {ECO:0000313|EMBL:RRA48797.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA48797.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Pold G., Deangelis K.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RRA48797.1, ECO:0000313|Proteomes:UP000279598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB88 {ECO:0000313|EMBL:RRA48797.1,
RC ECO:0000313|Proteomes:UP000279598};
RA Horta L.;
RT "Genome sequence of EB88, a novel member of the group I Acidobacteria.";
RL Submitted (DEC-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 -!- 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:RRA48797.1}.
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DR EMBL; QWEV01000005; RRA48797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P0X9H1; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000279598; 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:UP000279598};
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 18..202
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 364..368
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 553 AA; 60953 MW; 4051065C567183D9 CRC64;
MAEENVKLIP LGGLGEFGMN CMAVRYGNDI LVIDAGLMFP ESELLGVDIV VPDISYLVEN
RAHVRGILLT HGHEDHIGGL PWILSEINVP VYGTEFTLAY VEGKLDEHKM LDNTELIEIA
PNHKFQIGAF TIEPIRVTHS MVDCVALAIE TPVGVIVHTG DFKIDLSPPD GKAFDLHKFA
EYGQKGVLAL LQDSTNVDRP GYTPSEWAVK PRLDEVFQRT KKKLFFSCFS SSIYRIQIAL
DLAHKHGRKV AVVGRSMMES SEIAQDLGYL NLPPGLMIHP GQIGDHSPEN VMVLISGTQG
EPMSALSRAA VDNHKHARIS KGDTVLLSSR VIPGNEKSIY RVIDHLYRRE AEILYDDGTM
GLIHVSGHAS QEEQRLLINL LRPKFFIPVH GDFRHLKKHC ELALSTGVVG EAILIEDGDV
LELSATKARK AGKVTAGRVC IDSGSTADVV GDMVIRDRRN LSEDGIILPI LTINKLTGKV
ERQPEVVTRG FIGADAAVLR EAANIITQTL DSSSAEEKAD PGVMKEKIRI DLKRYIQKHT
SRRPLIMPVI LEV
//
