ID A0A344TXA6_9ACTN Unreviewed; 561 AA.
AC A0A344TXA6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=C0216_07240 {ECO:0000313|EMBL:AXE23277.1};
OS Streptomyces globosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68209 {ECO:0000313|EMBL:AXE23277.1, ECO:0000313|Proteomes:UP000252004};
RN [1] {ECO:0000313|EMBL:AXE23277.1, ECO:0000313|Proteomes:UP000252004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZH-48 {ECO:0000313|EMBL:AXE23277.1,
RC ECO:0000313|Proteomes:UP000252004};
RA Ran K., Li Z., Wei S., Dong R.;
RT "Draft genome Sequence of streptomyces globosus LZH-48.";
RL Submitted (JAN-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}.
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DR EMBL; CP030862; AXE23277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344TXA6; -.
DR KEGG; sgz:C0216_07240; -.
DR OrthoDB; 9770211at2; -.
DR Proteomes; UP000252004; Chromosome.
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:UP000252004};
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 31..228
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 373..377
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 561 AA; 61019 MW; 97ED334DFF0B1B0C CRC64;
MSHPHPELGP PPKLPQGGLR VTPLGGLGEI GRNMTVFEFD GRLLIVDCGV LFPEEEQPGI
DLILPDFSSI RDRLDDIEGI VLTHGHEDHI GAVPYLLREK PDIPLIGSKL TLALIEAKLQ
EHRIRPYTLE VKEGDRENLG VFDCEFIAVN HSIPDALAVA IRTPAGLVVA TGDFKMDQLP
MDNRLTDLHA FARLSEEGID LLLSDSTNAE VPGFVPPERD ISNVIRGVFA GAQRRIIVAS
FASHVHRIQQ VLDAAHEYGR RVAFVGRSMV RNMGIARDLG YLRIPQGLVV DVKTLDDLPD
DEVVLVCTGS QGEPMAALSR MANRDHQIRI VPGDTVILAS SLIPGNENAV YRVINGLTRW
GANVVHKGNA KVHVSGHASA GELLYFYNIC KPKNLMPVHG EWRHLRANAE LGAMTGVPKD
RIVIAEDGVV VDLVDGKARI SGKVQAGYVY VDGLSVGDVT ETSLKDRRIL GEEGIISVYV
VVDSTTGKVV SGPNIQARGS GIEDSAFTAV LPKIEEAIAR AAADGVAEPH QIQQLIRRTV
GKWVSDGYRR RPMILPVVVE V
//
