ID A0A239U564_9STAP Unreviewed; 557 AA.
AC A0A239U564;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=rnj2 {ECO:0000313|EMBL:GEP84280.1};
GN Synonyms=rnj {ECO:0000256|HAMAP-Rule:MF_01491};
GN ORFNames=SPI02_08650 {ECO:0000313|EMBL:GEP84280.1};
OS Staphylococcus piscifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=70258 {ECO:0000313|EMBL:GEP84280.1, ECO:0000313|Proteomes:UP000321736};
RN [1] {ECO:0000313|EMBL:GEP84280.1, ECO:0000313|Proteomes:UP000321736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109625 {ECO:0000313|EMBL:GEP84280.1,
RC ECO:0000313|Proteomes:UP000321736};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Staphylococcus piscifermentans NBRC
RT 109625.";
RL Submitted (JUL-2019) 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:GEP84280.1}.
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DR EMBL; BKAR01000008; GEP84280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239U564; -.
DR OrthoDB; 9758375at2; -.
DR Proteomes; UP000321736; 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:SF4; RIBONUCLEASE J 2; 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|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 RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01491};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01491}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 23..217
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; 62458 MW; 838B419BE1913113 CRC64;
MNLVKKKNND IRIIPLGGVG EIAKNMYIVE VDDEMFMLDA GLMFPEDEML GVDVVIPDIQ
YVIENKDKLK GIFLTHGHEH AIGAVSYVLE QVDAPVYGSK LTLALVKENM KERNINKKVR
YYTVNDESVM RFKNVNVSFF NTTHSIPDSL GVIIHTSYGA IVYTGEFKFD QSLHGNYAPD
LKKMTEIGEE GVFALISDST EAEKPGYNTP ENVIESHMLD AFTKVNGRLI VSCYASNFIR
IQQVLNIASK LNRKVSFLGR SLESSFNIAR KMGYFNIPKD LLIPINEVEN YPKNEVVIIA
TGMQGEPVEA LNQMARQKHK IMNIEPGDSV FLAITASANM EVIIGDTLNE LARAGAEIIP
NSKKIHASSH GCMEELKMMI NIMKPEYFIP VQGEFKMQIA HAKLAAEAGV APEKIFLAEK
GDVLNFDGKD MVLNEKVESG NVLIDGIGVG DVGNIVLRDR HLLAEDGIFI AVVTLDPKNR
RIAAGPEIQS RGFVYVRESE ELLKEAEEKV REIVEQGLQE RRIEWSEIKQ NMRDKISKLL
FENTKRRPMI IPIISEV
//
