ID E3C981_9LACO Unreviewed; 611 AA.
AC E3C981;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=HMPREF9265_1003 {ECO:0000313|EMBL:EFQ52693.1};
OS Limosilactobacillus oris PB013-T2-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ52693.1, ECO:0000313|Proteomes:UP000003070};
RN [1] {ECO:0000313|EMBL:EFQ52693.1, ECO:0000313|Proteomes:UP000003070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ52693.1,
RC ECO:0000313|Proteomes:UP000003070};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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:EFQ52693.1}.
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DR EMBL; AEKL01000063; EFQ52693.1; -; Genomic_DNA.
DR RefSeq; WP_003713693.1; NZ_AEKL01000063.1.
DR AlphaFoldDB; E3C981; -.
DR eggNOG; COG0595; Bacteria.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000003070; 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|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW 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 23..218
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT REGION 565..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 368..372
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 611 AA; 68518 MW; 65A860540B9CC8F4 CRC64;
MAKLKIKNNE VAFYAMGGLG EIGKNMYCVQ FQDEIIIIDC GVLFPEDELL GVDYVIQNYD
YLIENKDKIK GIFITHGHED HIGGLPFFLQ KVNAPIYAGP FAMSLIKGKL EEKHLLRNAE
LHEINEFDEV HFKKLWVSFF RTTHSIPDTL GVAVHTPQGT IIQTGDFKFD LTPVGGLPGP
NLQQMAKLGD EGVLLLTSDS TNAERPQFTK SERWVDIHIR RIFERIKGRI IFASFASNVY
RLREASDAAI AQGRKIAVFG RSMENAIAAG QELGYLNIPE DALIDQNEIN NYPPEKVLIM
CTGSQGEPMA ALSRIANGTH RQITIQPDDT VVFSSNPIPG NTTSVNALIN KLEESGANVI
HGYVNNIHTS GHGGQIDEEF MLRLMKPKFF APVHGEYRMQ KIHTKLAELA GVPRENSFIL
ANGDVLALTK DSCRIADHID SVSDVYIDGR DAGDTVGNPE IRERRLLSEE GVVTAIAVVD
LKDYQIVAGP DIVSRGFVYM HESQELIKAA NHEVFWAILN TFKNHKHVDQ RALNRTIVSR
LQKLLFERTG RRPVIIPMVT ILNGNNRSEN HHYRHPNHNR RGKENEKRPA NHSKHEGKGN
GQQRKEEAVK A
//
