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Database: UniProt
Entry: R7H863_9FIRM
LinkDB: R7H863_9FIRM
Original site: R7H863_9FIRM 
ID   R7H863_9FIRM            Unreviewed;       556 AA.
AC   R7H863;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=BN634_02334 {ECO:0000313|EMBL:CDE35481.1};
OS   Eubacterium sp. CAG:38.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262889 {ECO:0000313|EMBL:CDE35481.1, ECO:0000313|Proteomes:UP000017954};
RN   [1] {ECO:0000313|EMBL:CDE35481.1, ECO:0000313|Proteomes:UP000017954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:38 {ECO:0000313|Proteomes:UP000017954};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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:CDE35481.1}.
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DR   EMBL; CBIU010000022; CDE35481.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7H863; -.
DR   STRING; 1262889.BN634_02334; -.
DR   Proteomes; UP000017954; 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|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   Reference proteome {ECO:0000313|Proteomes:UP000017954};
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         363..367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT                   ECO:0000256|PIRSR:PIRSR004803-2"
SQ   SEQUENCE   556 AA;  61382 MW;  15E9101C715F6168 CRC64;
     MKKEYVGSVK IIPLGGLDKI GMNITAIQYD DSIIVVDCGL AFPEEEMLGI DLVIPDVTYL
     KENADKVKGF VITHGHEDHI GSIPYVLKEV NAPIYATKLT MGLIDSKLKE HGMQRQVKRK
     VVRYGQSINL GDFRVEFIRT NHSIADAAAL AIFSPAGVII HTGDFKVDYT PVYGEPIDLQ
     RMGELGKKGV LALMCDSTNA LRPGFTMSER TVGATFDKIF TDNKNSRLII ATFASNVDRV
     QQIINSAVKY GRKVCVEGRS MVNIIEVAEN LDYLKIPEGT LIDTEEMKNY TPEQIVLITT
     GSQGESMAAL SRMAASLHRK VSIQPGDCVV FSSTPIPGNE KSVAKVINEL GMKGAKVIFQ
     DTHVSGHACQ EEIKLLYSLI KPKYAIPVHG EYRHLMAQKE VVQSLGYDKE DIFIAKCGDV
     LELSEEKAGI VGHVQTGEIL VDGLGVGDVG NIVLRDRQNL AENGIIIVVL TLEKYSGQLV
     AGPDIVTRGF VYVREAEELL DEAREVVSGS VETCMDKNIT DWSKIKNIIK DDLSEYLWKK
     MKRNPVILPI IMEAHM
//
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