ID A0A1E5Q0C1_9ACTN Unreviewed; 561 AA.
AC A0A1E5Q0C1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=BGK67_31615 {ECO:0000313|EMBL:OEJ35247.1};
OS Streptomyces subrutilus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36818 {ECO:0000313|EMBL:OEJ35247.1, ECO:0000313|Proteomes:UP000095705};
RN [1] {ECO:0000313|EMBL:OEJ35247.1, ECO:0000313|Proteomes:UP000095705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-1-1 {ECO:0000313|EMBL:OEJ35247.1,
RC ECO:0000313|Proteomes:UP000095705};
RA Chen X.;
RT "The complete genome of Streptomyces subrutilus 10-1-1.";
RL Submitted (AUG-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:OEJ35247.1}.
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DR EMBL; MEHK01000001; OEJ35247.1; -; Genomic_DNA.
DR RefSeq; WP_069923433.1; NZ_MEHK01000001.1.
DR AlphaFoldDB; A0A1E5Q0C1; -.
DR STRING; 36818.BGK67_31615; -.
DR OrthoDB; 9770211at2; -.
DR Proteomes; UP000095705; 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:UP000095705};
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; 60699 MW; E6CE3F5E55E82E16 CRC64;
MSHPHPELQA APPLPAGGLR VTALGGLGEI GRNMTVFEHA GKLLIVDCGV LFPEEHQPGV
DVILPDFTSI RDRLDDIVAV VLTHGHEDHI GGVPYLLRER ADIPVVGSKL TLAFLEAKLK
EHGIKPRTAR VREGDRRRFG PFDCEFVAVN HSIPDGLAVA IRTGAGMVLH TGDFKMDQFP
LDERITDLRA FARLGEEGVD LFLTDSTNAE VPGFTTSERE LNPAIEQVLR TAPRRVIVSS
FASHVHRIQQ VLDAAHQHGR KVAFVGRSMV RNMGIARELG YLKVPAGLVV SMKELEQLPD
NKITLVCTGS QGEPMAALSR MANRDHQIRI GKGDTVLLAS SLIPGNENAI YRIINGLTRW
GANVVHKGNA KVHVSGHASA GELVYCYNIV KPRNVMPVHG EWRHLRANAD LAIRTGVDPD
RVVIAEDGVV VDLVDGHAKI TGKVPAGYVY VDGMTVGGAT EASLKDRVTL AQEGVVTVVA
IVDANTGMLA EAPDFLARGF EHDDTTFAAV IPVIEKTLAT AAKEGVGDAV QLEQLIARAV
ANWAFRTHRR KPLIIPVIID A
//