ID A0A3G9A138_9ACTN Unreviewed; 544 AA.
AC A0A3G9A138;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EH165_07905 {ECO:0000313|EMBL:AZI59491.1};
OS Nakamurella antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC Nakamurella.
OX NCBI_TaxID=1902245 {ECO:0000313|EMBL:AZI59491.1, ECO:0000313|Proteomes:UP000268084};
RN [1] {ECO:0000313|EMBL:AZI59491.1, ECO:0000313|Proteomes:UP000268084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-144 {ECO:0000313|EMBL:AZI59491.1,
RC ECO:0000313|Proteomes:UP000268084};
RA Da X.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AZI59491.1, ECO:0000313|Proteomes:UP000268084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-144 {ECO:0000313|EMBL:AZI59491.1,
RC ECO:0000313|Proteomes:UP000268084};
RA Peng F.;
RT "Nakamurella antarcticus sp. nov., isolated from Antarctica South Shetland
RT Islands soil.";
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}.
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DR EMBL; CP034170; AZI59491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9A138; -.
DR KEGG; nak:EH165_07905; -.
DR OrthoDB; 9770211at2; -.
DR Proteomes; UP000268084; 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 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:UP000268084};
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 13..207
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 356..360
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 544 AA; 58494 MW; B0E9B3D70B85C0A5 CRC64;
MRIVALGGIG EIGRNMTVYE YRGKLLIVDC GVLFPEATEP GVDLILPDFS YIEDRVQDIE
AVVITHGHED HIGALPFLLR LRRDLPVLGA TFSNALIAAK CKEHRINPKL QTVREGDLLS
VGAFDLEFFA VNHSIPDALA VGIRTPAGTV LHTGDIKLDQ LPLDGRLTDL GGFSRFGEEG
VDLFMVDSTN AEVPGFVAPE REIGPVLDRF IASAKQRVIV ASFASHVHRI QQVVDAAQRH
GRKIAFVGRS MVRNMQIAQE LGFLTVPDGL IRSMDKILDL APDKVVLIST GSQGEPLSAL
SRMARGDHRQ VNLVAGDTVI LASSMIPGNE TSVFTVVNEL ARIGVQVVHQ GMAKVHVSGH
ASAGELLYLY NAVKPKNVIP VHGEWRHLRA NAALAALTGV PKDRILMAPD GVVVDLIKGK
ASVVGMIEVG HVYVDGNSVG DVGDATLSDR LVLGEGGFIS VTVAIDATTG RAVSPPTVSG
RGFSDDPNAL DAVVPLVEME LARSENDGIV DPHRIAQAVR RIVGRWVGDT YRRRPMIIPT
IITV
//
