ID A0A2L2BRQ2_9MICO Unreviewed; 559 AA.
AC A0A2L2BRQ2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=C3B54_111395 {ECO:0000313|EMBL:AVG24338.1};
OS Pontimonas salivibrio.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Pontimonas.
OX NCBI_TaxID=1159327 {ECO:0000313|EMBL:AVG24338.1, ECO:0000313|Proteomes:UP000243077};
RN [1] {ECO:0000313|EMBL:AVG24338.1, ECO:0000313|Proteomes:UP000243077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL-TW6 {ECO:0000313|EMBL:AVG24338.1,
RC ECO:0000313|Proteomes:UP000243077};
RA Cho B.C., Hardies S.C., Jang G.I., Hwang C.Y.;
RT "Complete genome of the streamlined marine actinobacterium Pontimonas
RT salivibrio CL-TW6 adapted to coastal planktonic lifestype.";
RL Submitted (FEB-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; CP026923; AVG24338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L2BRQ2; -.
DR KEGG; psai:C3B54_111395; -.
DR OrthoDB; 9770211at2; -.
DR Proteomes; UP000243077; 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:UP000243077};
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 28..222
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 371..375
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 559 AA; 60414 MW; 0E5CB23B15A4E8D9 CRC64;
MAQPLLDPPA LNSETLRIIP LGGIGEVGRN MTVFELGGKL LVVDAGVLFP EETQPGVDLI
LPDFAPIRDR IDDIEAIVLT HGHEDHIGAV PYLLKIRDDI PLVGSTLTMA LIEAKLKEHR
ITPYTLTVSE GTREKLGPFD VEFLAVNHSI PDALALFIRT TAGTVLHTGD FKMDQLPLDG
RLTDLRGFAR VGEEGVDLLM ADSTNADIPG FTPAERGIGP VLEQVVHHAK RRVIVASFSS
HVHRVQQVID SAVANGRRVA LVGRSMVRNM GIAKELGFLR VPEGALIDAK KAPDMPDDKI
VYMTTGSQGE PMAGLSRMAN REHPTIAIGE GDTVILASSL IPGNENAVYR VINGLIDLGA
QVIHKGNAKV HVSGHAAAGE LLYVYNLVQP RHVMPIHGEA RHLRANAEVA VDSGVPRDNV
MICENGSVVD LVEGRAKQTG QIDIGFVYVD GSTVGEITDA DLKDRRILAE EGFISIFLAI
DAQTGKIIVG PEIHARGFAP DDSVFDDVRP AILKALEEAA GQGTRDPHGF SQVVRRVVGR
WVNTQHRRRP MIVPIVIEA
//
