ID Q9CF63_LACLA Unreviewed; 570 AA.
AC Q9CF63;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=yqgA {ECO:0000313|EMBL:AAK05716.1};
GN Synonyms=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN ORFNames=L61727 {ECO:0000313|EMBL:AAK05716.1};
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623 {ECO:0000313|EMBL:AAK05716.1, ECO:0000313|Proteomes:UP000002196};
RN [1] {ECO:0000313|EMBL:AAK05716.1, ECO:0000313|Proteomes:UP000002196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403 {ECO:0000313|EMBL:AAK05716.1,
RC ECO:0000313|Proteomes:UP000002196};
RX PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01491}.
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DR EMBL; AE005176; AAK05716.1; -; Genomic_DNA.
DR PIR; B86827; B86827.
DR RefSeq; NP_267774.1; NC_002662.1.
DR RefSeq; WP_003129410.1; NC_002662.1.
DR AlphaFoldDB; Q9CF63; -.
DR PaxDb; 272623-L61727; -.
DR EnsemblBacteria; AAK05716; AAK05716; L61727.
DR GeneID; 69713698; -.
DR KEGG; lla:L61727; -.
DR PATRIC; fig|272623.7.peg.1739; -.
DR eggNOG; COG0595; Bacteria.
DR HOGENOM; CLU_008727_3_1_9; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000002196; 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 NCBIfam; TIGR00649; MG423; 1.
DR PANTHER; PTHR43694; RIBONUCLEASE J; 1.
DR PANTHER; PTHR43694:SF4; RIBONUCLEASE J 2; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR Pfam; PF17770; RNase_J_C; 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|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 Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01491};
KW Reference proteome {ECO:0000313|Proteomes:UP000002196};
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 16..212
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 570 AA; 63525 MW; 97C61E0AE6C705BE CRC64;
MSNIKITPLG GVREFGKNMY LVEVEEQIFV LDAGLKYAEM DQLGVDFVIP DITYLLENAD
RVAGIFLTHG HADSIGALPY IVSELKVPVF GSELTIELAK INVKNYADSR KFNDFHVVTE
DTEIDFGKAV ISFFSTTHTI PESLGIVIST NDGNIVYTGD FRFDPAVAKG YRTNMRRLAE
IGNSGVLALL SSSPNALSTM QSASEHEIYE KIYDYIDDNE GRVIIACNAG NLGRIQQTID
AAIKLGRRVA FTGEDMDQII ETATRLNKLQ IVDKKSIIKP AEIKKYADNE LVILETGRMG
EPLKSLGDMA HRRHKYVKIK DGDLVLAVTS PSVSYETTIA RIENEIYKAG GVMKMLASDL
KISGHANARD LQFLLDIFRP KNLIPIQGEY RELSAHADLA MEMDILPEHI FIAKRGETVS
LENGDMIPSG VIQAENVMID GSGVGDIGSV VLRDRKVLSE DGIFIAVITI SKTERKIVSK
SRVHTRGFVY VKTSRDLMRE AGELVNETVD KYLSGKEFDW AEIKGSIRDA LGKFLYEQTK
RKPVILPVVM EARQPQDLNK RYTKKNHNKK
//
