ID A0A1Y1RN70_9MICC Unreviewed; 571 AA.
AC A0A1Y1RN70;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=A7979_07520 {ECO:0000313|EMBL:ORC15568.1};
OS Rothia nasimurium.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=85336 {ECO:0000313|EMBL:ORC15568.1, ECO:0000313|Proteomes:UP000192359};
RN [1] {ECO:0000313|EMBL:ORC15568.1, ECO:0000313|Proteomes:UP000192359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PT-32 {ECO:0000313|EMBL:ORC15568.1,
RC ECO:0000313|Proteomes:UP000192359};
RA Gaiser R.A., Van Baarlen P., Wells J.M.;
RT "Draft genome sequence of a porcine commensal Rothia nasimurium.";
RL Submitted (MAY-2016) 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:ORC15568.1}.
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DR EMBL; LXWF01000043; ORC15568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1RN70; -.
DR OrthoDB; 9770211at2; -.
DR Proteomes; UP000192359; 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 Reference proteome {ECO:0000313|Proteomes:UP000192359};
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 30..224
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 372..376
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 571 AA; 62734 MW; CF10BE17E1FB3F59 CRC64;
MQTVTSPHLP PKLRKDTLRV IPLGGLGEVG RNMTVYEING KLLVVDCGVL FPEESQPGVD
LILPDLNYIK NRLQDIVAIV LTHGHEDHIG AVPYLLRLRP DIPLVGSQLT LALIEAKLQE
HRIKPYTMDV VEGQVERFGP FECEFVAVNH SIPDALAVFI RTKAGKALHT GDFKMDQLPL
DGRLTDLRHF ARLGEEGIDL FLPDSTNAEV PGFTPTEKNI GPVISNVIRD AKRRVIVASF
SSHVHRVQQV LDAAAERGRK VVLVGRSMVR NMTIAEKLGY LNVPEGILVD LKKVDDYRPE
QIVMMCTGSQ GEPMAALSRM ANGDHKIQVE KGDTIILASS LIPGNETSVY RVINGLMKLG
ANVVHKGTAK VHVSGHAAAG ELLYCYNILQ PANVMPVHGE VRHLLASGKL AVETGIKSDR
VLICDSGTVV DLRDGRAEIV GQVPCEYVYV DGKSVGHVTE DDLKDRRVLG EEGFVSIVTV
VDRATKRVVT GPDIHARGIA EDDSVFNDIT PKITVALEDA LHRAPERVHT THQLQQIVRR
TMGAWVARRL RRKPMIVPVV IETHTPEAEG N
//
