ID A0A1D7YK82_9ACTN Unreviewed; 561 AA.
AC A0A1D7YK82;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=BFF78_37280 {ECO:0000313|EMBL:AOR35961.1}, BFF78_41895
GN {ECO:0000313|EMBL:AOR36738.1};
OS Streptomyces fodineus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR35961.1, ECO:0000313|Proteomes:UP000094960};
RN [1] {ECO:0000313|Proteomes:UP000094960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA Kim M.-K., Kim S.B.;
RT "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AOR35961.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TW1S1 {ECO:0000313|EMBL:AOR35961.1};
RA Kim M.-K., Kim S.B.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AOR35961.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TW1S1 {ECO:0000313|EMBL:AOR35961.1};
RX PubMed=30896386;
RA Kim M.K., Kang H.J., Roh S.G., Park J.S., Kim S.B.;
RT "Streptomyces fodineus sp. nov., an actinobacterium with antifungal
RT activity isolated from mine area soil.";
RL Int. J. Syst. Evol. Microbiol. 69:1350-1354(2019).
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; CP017248; AOR35961.1; -; Genomic_DNA.
DR EMBL; CP017248; AOR36738.1; -; Genomic_DNA.
DR RefSeq; WP_069782475.1; NZ_CP017248.1.
DR AlphaFoldDB; A0A1D7YK82; -.
DR KEGG; spun:BFF78_37280; -.
DR KEGG; spun:BFF78_41895; -.
DR Proteomes; UP000094960; 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 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..225
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; 60691 MW; B6F3F076E23EE8D8 CRC64;
MSHPHPELKA APPLPEGGLR VIALGGLGEI GRNMTVFEHA GKLLIVDCGV LFPEETQPGV
DVILPDFTSI RDRLDDIVAV VLTHGHEDHI GGVPYLLRER SDIPVVGSKL TLAFLEAKLK
EHGIRPRTVP VREGDRRGFG PFDCEFVAVN HSIPDSLAVA IRTRAGMVLH TGDFKMDQFP
LDDRITDLRA FARLGEEGVD LFLTDSTNAE VPGFTTSERE LNPAIEQVMR TAPRRVIVSS
FASHVHRIQQ VLDAAHQHGR KVAFVGRSMV RNMGIARDLG YLKVPSGLVV STKELEKLPD
HKITLVCTGS QGEPMAALSR MANRDHMIRI GKGDTVLLAS SLIPGNENAI YRVINGLTRW
GAHVVHKGNA KVHVSGHASA GELVYCYNIV KPRNVMPVHG EWRHLRANGD LAIRTGVDPE
RVVLAEDGVV VDLVDGRASI TGKVPAGNVY VDGMEVGGAT EASLKDRLTL AAEGVVTVVA
IVDADTGALA EAPDFLARGF VHDDATFEPV IPVIEKTLAT AAEEGVGDAH QLEQLVARAV
ANWAFRTHRR KPLIIPVIID A
//
