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Database: UniProt
Entry: A0A024QCK0_9BACI
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ID   A0A024QCK0_9BACI        Unreviewed;       555 AA.
AC   A0A024QCK0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=rnjA {ECO:0000313|EMBL:CDQ40268.1};
GN   Synonyms=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN   ORFNames=BN990_02588 {ECO:0000313|EMBL:CDQ40268.1};
OS   Virgibacillus massiliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ40268.1, ECO:0000313|Proteomes:UP000028875};
RN   [1] {ECO:0000313|EMBL:CDQ40268.1, ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ40268.1,
RC   ECO:0000313|Proteomes:UP000028875};
RA   Urmite Genomes U.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA   Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT   "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL   Submitted (MAY-2014) 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:CDQ40268.1}.
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DR   EMBL; CCDP010000001; CDQ40268.1; -; Genomic_DNA.
DR   RefSeq; WP_021291731.1; NZ_WMER01000002.1.
DR   AlphaFoldDB; A0A024QCK0; -.
DR   STRING; 1462526.BN990_02588; -.
DR   eggNOG; COG0595; Bacteria.
DR   OrthoDB; 9758375at2; -.
DR   Proteomes; UP000028875; 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:UP000028875};
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;  61260 MW;  8291CE998DF691E3 CRC64;
     MKFVKNDQAA VFALGGLGEI GKNTYGVQFQ DEIILIDAGI KFPEDELLGI DYVIPDYTYL
     VQNQDKIKGL FITHGHEDHI GGIPYLLREI NVPIYAGKLA IGLIRNKLDE HGLLRNAKLN
     TIQEDDIIKF RKTSVSFFLT THSIPDAYGI VVKTPPGNIV HTGDFKFDFT PVGEPANLSK
     MAEIGNEGVL CLLSDSTNSE VPGFTMSEKV VGSNIKDIFS RVDGRVIFAT FASNIYRLQQ
     VVEAAVKNNR KIAVFGRSME SAINLGQELG YIQAPKNTFI DANQINRLPA QEVTILCTGS
     QGEPMAALSR IANGTHRQIQ IIPGDTVVFS SSPIPGNTIS VGRTINKLYR AGADVIHGKL
     SNIHTSGHGS QEEQKLMLRL IKPKHFMPIH GEYRMLKEHM KLAESCDVEP ANSFIMDNGD
     VLALGKDTAI IAGKIPSGSI YVDGSGIGDI GNIVLRDRRI LSEEGLVIVV VSINMKEFKI
     SAGPDIISRG FVYMRESEDL INEAQKLVSN HLDKVMERKT SQWSEIKNEI TDTIAPFLYE
     KTKRRPMVLP IIMEV
//
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