ID A0A1Y4EWR7_9FIRM Unreviewed; 630 AA.
AC A0A1Y4EWR7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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=B5F54_02470 {ECO:0000313|EMBL:OUO75917.1};
OS Anaeromassilibacillus sp. An250.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaeromassilibacillus.
OX NCBI_TaxID=1965604 {ECO:0000313|EMBL:OUO75917.1, ECO:0000313|Proteomes:UP000195568};
RN [1] {ECO:0000313|Proteomes:UP000195568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An250 {ECO:0000313|Proteomes:UP000195568};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO75917.1}.
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DR EMBL; NFJK01000002; OUO75917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4EWR7; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000195568; 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:UP000195568};
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 95..293
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 440..444
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 630 AA; 69340 MW; CB5AB34534FF33EB CRC64;
MGIAAGIHPA LYGKVTLPQR PEQPIQAEAP AAKAEPSKRR TMRRAPKKAE PEKAQHQNSK
ETKAAAPRGK KRGQNSGAKK PSIRIYFLGG LNEIGKNFTL YECEGDMLIV DCGMSFPDDD
MLGVDLVLPD FTFVERNADK IRGIVLTHGH EDHIGALPYL LKRVNLPIYG TMLTLGLVDG
KLKEHGLSGK VKMNVVKPGQ TVKLGCMDVE FIHVNHSIPD SVGFAIHSPA GTVVYTGDFK
IDCTPAWGEM IDLGRFAELG NEGVLALLAD STNAERPGYT KTEQMVDNTF ESLFKKAEKK
RIIIATFASN ISRVQQIINC AVRYGRKVAL SGRSMLNVMG IAVEMGYLQV PDGVLIDIDL
LNRYPREKVV LITTGSQGEP MSALTRMAFA DHRKVEVGPE DFIIISARPI PGNEKTVGAV
VDELLKRGCE VIYESMYEVH VSGHACQEEL KIIQGITKPK YFIPFHGEQK HLRKNAGLAI
SMGMDPANVY IGDIGDVLEI NHEYMKKLTS VPAGRILVDG LGVGDVGSIV LRDRKHLAED
GLIVVVCTID DNGQIVAGPD VVSRGFVYVR EAEPLIDEAK KRVAAALESC SEHHIHDWGT
LKTRIKDELS RFLYERTRRS PMILPIIMEV
//
