ID A0A1G2MSI3_9BACT Unreviewed; 560 AA.
AC A0A1G2MSI3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=A3C06_01250 {ECO:0000313|EMBL:OHA26803.1};
OS Candidatus Taylorbacteria bacterium RIFCSPHIGHO2_02_FULL_46_13.
OC Bacteria; Candidatus Taylorbacteria.
OX NCBI_TaxID=1802312 {ECO:0000313|EMBL:OHA26803.1, ECO:0000313|Proteomes:UP000177565};
RN [1] {ECO:0000313|EMBL:OHA26803.1, ECO:0000313|Proteomes:UP000177565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:OHA26803.1}.
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DR EMBL; MHRQ01000016; OHA26803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2MSI3; -.
DR STRING; 1802312.A3C06_01250; -.
DR Proteomes; UP000177565; 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 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 20..205
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 365..369
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 560 AA; 63259 MW; E878D3FABEDF546F CRC64;
MPPLGDSIRI IPLGGVEEIG KNMTAIEYGN DILVIDAGLQ FRDENTPGID FILPNTKYLE
ERRDRVRALV ITHGHLDHIG GIPYIMDKIG NPPLYSRMLT TVMIQKRQEE FPHAQPLDIK
VVEKDSVVQI GNFKVRFFSV THTIPDAMGV IVETPYGAIV NTGDLKVDHD NGIPTEREVK
EYEIFKHEKV LLLMADSTNT DVPGFSTPER LVQKNLEEII KNSKGRLIMA TFSSLLERIM
KIIEFAEKYN KKVVIEGRSM KNNVEIIKHL GMLKTKKETI ISVEAMDDYP PEKIVMIATG
AQGDEFAALM RMANKSHKYV RINKRDTIVL SSSIVPGNER AVQKLKDGLS RQGARILHYK
IADVHSSGHA NRDEMAWIHN KINPKFFMPI HGYHYMLRVH ADIELARGTP EKNIIIPDDG
SIIEIQDKGE KIVCLKEKAP SGLVMVDGFS VGDMQEVVIR DRQMLSQDGM FVIIASVNIA
NGRLKKSPDI ISRGFVYLRE SQDLLQQTRL IIKKTIEDIT VGMRPIDFEY VKDRVTDNVS
RFLLQKTAKR PIVIPVLIGA
//
