ID A0A327YTM9_9BACI Unreviewed; 555 AA.
AC A0A327YTM9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Ribonuclease J {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803};
DE Short=RNase J {ECO:0000256|HAMAP-Rule:MF_01491};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRNR:PIRNR004803};
GN Name=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN ORFNames=B0I26_101388 {ECO:0000313|EMBL:RAK23427.1};
OS Anoxybacillus vitaminiphilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=581036 {ECO:0000313|EMBL:RAK23427.1, ECO:0000313|Proteomes:UP000248555};
RN [1] {ECO:0000313|EMBL:RAK23427.1, ECO:0000313|Proteomes:UP000248555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8979 {ECO:0000313|EMBL:RAK23427.1,
RC ECO:0000313|Proteomes:UP000248555};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRNR:PIRNR004803};
CC Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or
CC Mg(2+) is physiologically important. {ECO:0000256|PIRNR:PIRNR004803};
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 ECO:0000256|PIRNR:PIRNR004803}.
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 ECO:0000256|PIRNR:PIRNR004803}.
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:RAK23427.1}.
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DR EMBL; QLMH01000001; RAK23427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327YTM9; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000248555; 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 InterPro; IPR001587; RNase_J_CS.
DR NCBIfam; TIGR00649; MG423; 1.
DR PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR PANTHER; PTHR43694:SF4; RIBONUCLEASE J 2; 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.
DR PROSITE; PS01292; UPF0036; 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 ECO:0000256|PIRNR:PIRNR004803};
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 21..216
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 364..368
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 555 AA; 61491 MW; EFDC43506830EB1F CRC64;
MSTKHAEKIR VFSLGGVGEI GKNMYVVEID DDIFVIDAGI MFPEGEMLGI DMVIPDISYL
VERQERIKGI FLTHGHEEHI GAIAYVLRKI NVPVYATKLT LALVEEKLKE HGVTVRAQLN
EVHSDSVVTF EKVKMTFFRT IHSIPDSIGI SIHTSQGAIV YTGDFKFDQT PYGINRVDLG
KMAQIGDQGV LCLLSDSTNA EKPGYTGSDA IVAQEIADVV YDAPGRVIVA CYASNITRIQ
QVLNAAKKHK RKVAIAGRSM HKVMDIALRL GYLQIPDKLV IPINDIHQYE DKELVILTTG
GHGEPMGVLA RMAKQAHKQV NIKEGDTVII AASPMPGNEL TVSRTIDALY RAGANVIYRQ
RNVHVSGHGS QEELKLMLNL MKPKYFIPVH GEYRMQKAHA KLAKAVGIAE DQTFLIDKGD
VIEFRNGQAR YGGKVPCGNI LIDGLGIGDV GNIVLRDRRL LSQDGILIVV VTLSKEAKKI
IAGPEIISRG FVYVRGSETL LDEATKIVTD IVNKCMQDYI IEWSSLKSNI REALNQYLFE
KTKRKPMILP IIMEI
//
