ID A0A1I2SFF6_9FIRM Unreviewed; 554 AA.
AC A0A1I2SFF6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05660649_01809 {ECO:0000313|EMBL:SFG48856.1};
OS Desulfotruncus arcticus DSM 17038.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC Desulfotruncus.
OX NCBI_TaxID=1121424 {ECO:0000313|EMBL:SFG48856.1, ECO:0000313|Proteomes:UP000199337};
RN [1] {ECO:0000313|Proteomes:UP000199337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17038 {ECO:0000313|Proteomes:UP000199337};
RA Varghese N., Submissions S.;
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 -!- 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}.
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DR EMBL; FOOX01000005; SFG48856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2SFF6; -.
DR STRING; 341036.SAMN05660649_01809; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000199337; 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 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.
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:UP000199337};
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 19..214
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 554 AA; 61770 MW; C89B797CF3989D19 CRC64;
MAREPKLYLI PLGGLGEIGK NMMVVRYGEN ILVIDSGLMF PEEDLLGIDM VIPDITYLLE
NKNIVRGIVL THGHEDHIGA LPYVLRELNV PVYGTRLTLG ILKEKLRERQ MADEVKLHCA
KPRDIISVGP FKIEFIRVSH SIPDAVSLAI ETPVGVVVHT GDFKLDQTPV DGEVTDFNRL
AQLGEKGVLV LLSDSTNVER PGYTLSEKVV GQTFDDSFRQ ASERIIVATF ASNVHRLQQA
ITTAHRYKRK VAVVGRSMVN VVNIARELGY LRVPEDVLVE LDEAGRLPRN RVVYLTTGSQ
GEPMSALTRM ANRDHRQVEI MPGDTIIISA TPIPGNEKLV ARVIDQLFKQ GANVIYESVS
GIHVSGHPSQ EELKLMFNLV KPKFFIPVHG EYRMLIKHAN LAREMGIPPN NIFVAENGQV
LEISRRSGRF AGRVTAGRVL VDGLGVGDVG NIVLRDRRQL SQDGILIVVV TISKESGQII
SGPDIVSRGF VYVRESEELM EDAKEKVKLA LDKCSAKKMS EWASIKSMVR DDLSRFLYEK
TRRRPMILPI IMEI
//
