ID A0A0T5XC11_9BACT Unreviewed; 602 AA.
AC A0A0T5XC11;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=HMPREF1705_03141 {ECO:0000313|EMBL:KRT35885.1};
OS Acetomicrobium hydrogeniformans ATCC BAA-1850.
OC Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae;
OC Acetomicrobium.
OX NCBI_TaxID=592015 {ECO:0000313|EMBL:KRT35885.1, ECO:0000313|Proteomes:UP000005273};
RN [1] {ECO:0000313|EMBL:KRT35885.1, ECO:0000313|Proteomes:UP000005273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1850 {ECO:0000313|Proteomes:UP000005273};
RA Gruening B.A., Erxleben A., Flemming S., Lucas X., Doering K.,
RA Weitnauer G., Bechthold A., Guenther S.;
RL Submitted (SEP-2012) 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:KRT35885.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACJX03000001; KRT35885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5XC11; -.
DR STRING; 592015.HMPREF1705_03141; -.
DR eggNOG; COG0595; Bacteria.
DR Proteomes; UP000005273; 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 50..245
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 395..399
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 602 AA; 66827 MW; A7E429ADD291F30D CRC64;
MEGDFVALHF DVEVKYLVQK NATKRRRRSP DERKSASLKF IPLGGVSGIG KNISVLEYGD
DILVIDCGLM FPDEEMLGVD FVIPDPAYLL ANKERIRGMV ITHGHDDHIG ALPYILPELD
CPIYATRLTL GLIRSRMEER APKYELKAKE IQAGDVIDLG CFKVQPFSVC HSIPDGVGYA
IHTPLGVVLH TGDFKLDPTP IDGRATDYAL LASLGTKGVL LMLSDSTNVE RDGFTPSERM
VGKTMEQTFR LYKNKRIIIS SFASNLHRVQ QVIETAVRFN RKVALIGRSM IANVARAREL
GYMDVDDDVF IQPSEIEGFP NNRLVVITTG SQGEPFSGLV LMSRGDHRFI KLGPKDLVVI
SALPIPGNER LVHRTINDLF KQGCEVIYEA EQNIHVSGHA SREELKMILS LIKPSYFVPL
HGEYRHLVKH KQLAEEMGVP AKNAFVMEEG DVLSITKRQA RISGKVPAGA YIVDGRTYGD
LKGGLLGERK DLAEEGVFCI SVVLDSSGNV IAPLSIESRG FLHRVDADEL YRQIEDAVEK
AVKAFAREKR DRKDEDLASR IRSAIKGVLR RYSLSSPVIL VLVNEVKENA ILSGLAGREF
AK
//
