ID A0A1L3MHK8_9MICO Unreviewed; 561 AA.
AC A0A1L3MHK8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=ASJ30_10135 {ECO:0000313|EMBL:APH01841.1}, IGS73_11570
GN {ECO:0000313|EMBL:QOK21771.1};
OS Janibacter indicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=857417 {ECO:0000313|EMBL:APH01841.1, ECO:0000313|Proteomes:UP000182938};
RN [1] {ECO:0000313|EMBL:APH01841.1, ECO:0000313|Proteomes:UP000182938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YFY001 {ECO:0000313|EMBL:APH01841.1,
RC ECO:0000313|Proteomes:UP000182938};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOK21771.1, ECO:0000313|Proteomes:UP000593998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TT2 {ECO:0000313|EMBL:QOK21771.1,
RC ECO:0000313|Proteomes:UP000593998};
RA Lee K., Ganzorig M.;
RT "Janibacter indicus TT2 genome sequence.";
RL Submitted (OCT-2020) 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; CP013290; APH01841.1; -; Genomic_DNA.
DR EMBL; CP062789; QOK21771.1; -; Genomic_DNA.
DR RefSeq; WP_072624998.1; NZ_CP062789.1.
DR AlphaFoldDB; A0A1L3MHK8; -.
DR KEGG; jte:ASJ30_10135; -.
DR Proteomes; UP000182938; Chromosome.
DR Proteomes; UP000593998; 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:UP000182938};
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; 60935 MW; ECAAA55D188B2059 CRC64;
MSHPHPELEL PPPLADGALR VVALGGLGEV GRNMAVVEHQ GQLLIIDCGV LFPEDHQPGV
DLILPDFEYI LDRLDDVQAI VLTHGHEDHI GAVPYLLKHK PDIPLVGSML TLALIEAKLK
EHRIKPFTLG VKEGGRESFG VFDCEFIAVN HSIPDALAVF VRTDGGTLLH TGDFKMDQLP
LDRRLTDLRA FARVGEEGVD LFLTDSTNAE VPGFTTPERE IGPAIDTVFR NARRRIIVAC
FSSHVHRVQQ VLDAAERNGR KVAMVGRSMV RNMGIAADLG YLKVPDRVLV DVKKLDNYPD
DEVVLICTGS QGEPMAALSR MANRDHRIDV GDGDTVLLAS SLIPGNENAV YRVINGLMRL
GADVVHKGNA KVHVSGHASA GELLYCYNIV KPRNVMPVHG EWRHLVANAD LAIQTGVDPD
HVVLAEDGVV VDLVDGRARI TGAVPCGYVY VDGSSVGGAT EELLKDRRIL RDEGFISVMV
VVDSSTGKVI AGPEITARGF AEDDEIFTQV KPKIIAALDE AARKGTTDTH QLQQVVRRAV
GGWVGGKIRR RPMIIPVVVE A
//
