ID A0A1I6ACD3_9BACI Unreviewed; 555 AA.
AC A0A1I6ACD3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN04488577_0878 {ECO:0000313|EMBL:SFQ66404.1};
OS Bacillus sp. cl95.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ66404.1, ECO:0000313|Proteomes:UP000199578};
RN [1] {ECO:0000313|EMBL:SFQ66404.1, ECO:0000313|Proteomes:UP000199578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL95 {ECO:0000313|EMBL:SFQ66404.1,
RC ECO:0000313|Proteomes:UP000199578};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOYF01000001; SFQ66404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6ACD3; -.
DR STRING; 1761761.SAMN04488577_0878; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000199578; 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: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.
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 Reference proteome {ECO:0000313|Proteomes:UP000199578};
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..215
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; 61407 MW; 355ACA185BAAD153 CRC64;
MKFVKNDQTA VFALGGLGEI GKNTYAVQFQ DEIILIDAGI KFPEDELLGI DYVIPDYTYL
VKNEDKIKGL FVTHGHEDHI GGIPYLLKQV NIPIYGGKLA LGLIKNKLEE HGLLRSTKLI
EIKEDDIIKF RKTSVTFFRT THSIPDSYGI VVKTPPGQVV HTGDFKFDFT PVGEPANLTK
MAEIGKEGVL CLLSDSTNSE VPNFTMSERR VGESIQDVFR KVDGRIIFAT FASNIHRLQQ
VVEAAVMHGR KVAVFGRSME AAINIGLELG YITAPKETFI EAQQINRLPA NKVTILCTGS
QGEPMAALSR IANGTHRQIQ IIPGDTVVFS SSPIPGNTIS VSRTINMLFK AGAEVIHGSL
SDIHTSGHGG QEEQKLMLRL IKPKFFMPIH GEYRMQRMHA KLAVDCGVPE ENCFIMDNGE
VLALSDDTGQ VAGKIPSGNV YIDGSGIGDI GNIVLRDRRI LSEEGLVVVV VSINMKDFKI
SAGPDIISRG FVYMRESGDL INDAQSLITK HLNKVMERRT TQWSEIKNEI TDTLSPFLYE
KTKRRPMILP IIMEV
//