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Database: UniProt
Entry: N0AZT1_9BACI
LinkDB: N0AZT1_9BACI
Original site: N0AZT1_9BACI 
ID   N0AZT1_9BACI            Unreviewed;       557 AA.
AC   N0AZT1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=B1NLA3E_08640 {ECO:0000313|EMBL:AGK53490.1};
OS   Bacillus sp. 1NLA3E.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK53490.1, ECO:0000313|Proteomes:UP000013300};
RN   [1] {ECO:0000313|EMBL:AGK53490.1, ECO:0000313|Proteomes:UP000013300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1NLA3E {ECO:0000313|EMBL:AGK53490.1};
RX   PubMed=23833140;
RA   Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA   Brooks S., Kostka J.E., Green S.J.;
RT   "Genome sequences for three denitrifying bacterial strains isolated from a
RT   uranium- and nitrate-contaminated subsurface environment.";
RL   Genome Announc. 1:e00449-13(2013).
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; CP005586; AGK53490.1; -; Genomic_DNA.
DR   RefSeq; WP_015593549.1; NC_021171.1.
DR   AlphaFoldDB; N0AZT1; -.
DR   STRING; 666686.B1NLA3E_08640; -.
DR   KEGG; baci:B1NLA3E_08640; -.
DR   eggNOG; COG0595; Bacteria.
DR   HOGENOM; CLU_008727_3_1_9; -.
DR   OrthoDB; 9758375at2; -.
DR   Proteomes; UP000013300; Chromosome.
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 J2; 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:UP000013300};
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..214
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   BINDING         366..370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT                   ECO:0000256|PIRSR:PIRSR004803-2"
SQ   SEQUENCE   557 AA;  61494 MW;  0BD8F28E3EFED6F1 CRC64;
     MATTENKLSI FALGGINEIG KNMYVIQYAN DIIIVDCGGK FPDESLLGID LIIPDITYLE
     ENQDKIRALI VTHGHEDHIG GVPFFLKKLN VPIYATRFTL GLIELKLDEH KLRRDTQLVQ
     INSDSNLELG EINVSFFRVS HSIPDCLGVV FHTPEGNVVH TGDFKFDLTP VNSQHSDIHK
     MAEIGNQGVL VLISESTNAE RSGLTPSEQI IGGHMDEAFM KADGKIFIST FASNVNRLQQ
     VVEASIKTNR KLALLGRSMV NVVSVAIEHG YLNVPEGMLI EANEVDKLAP EKVTILCTGS
     QGEPNAALAR LASGNYRDAA IYPGDTVIFA ASPIPGNEKD VSRIIDNLFQ LGAKVVYGSG
     SSTGMHVSGH GYQEDLKLML TLMKPTYFIP IHGEYRMLHH HRLLAESVGI EKGNTFNIKN
     GDVVDVENSV ARQTRQVPSG VTYVDGMGVG DVGEIVLRDR KQLSEDGMLV IVLTISKTDR
     KIIQGPDTIS RGFVYVKDSE DLIKEINRLV KKSVNDLQAE NVRQWNVIKQ SIKKSVGQYL
     YSQTKRKPMI LPIIIEI
//
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