ID D9XV61_9ACTN Unreviewed; 561 AA.
AC D9XV61;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=SSRG_01567 {ECO:0000313|EMBL:EFL38763.1};
OS Streptomyces griseoflavus Tu4000.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL38763.1, ECO:0000313|Proteomes:UP000002968};
RN [1] {ECO:0000313|EMBL:EFL38763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL38763.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL Submitted (FEB-2009) 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; GG657758; EFL38763.1; -; Genomic_DNA.
DR RefSeq; WP_004924713.1; NZ_GG657758.1.
DR AlphaFoldDB; D9XV61; -.
DR STRING; 467200.SSRG_01567; -.
DR eggNOG; COG0595; Bacteria.
DR HOGENOM; CLU_008727_3_1_11; -.
DR OrthoDB; 9770211at2; -.
DR Proteomes; UP000002968; 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 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 31..225
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT BINDING 373..377
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01491,
FT ECO:0000256|PIRSR:PIRSR004803-2"
SQ SEQUENCE 561 AA; 61257 MW; 4B0A83A8C45EB2D6 CRC64;
MSHPHPELRP PSRLPKGGLR VTPLGGLGEI GRNMTVFEYG GRLLIVDCGV LFPEEEQPGI
DLILPDFTSI RDRLDDIEGI VLTHGHEDHI GGVPFLLREK PDIPLIGSKL TLALIEAKLQ
EHRIRPYTLE VAEGQRERVG PFDCEFIAVN HSIPDALAVA IRTPAGMVVH TGDFKMDQLP
LDNRLTDLHA FARLSEEGID LLLSDSTNAE VPGFVPPERD ISNVLRQVFA GARKRIIVAS
FASHVHRIQQ ILDAAHEYGR RVAFVGRSMV RNMGIARDLG YLKVPPGLVV DVKTLDDLPD
SEVVLVCTGS QGEPMAALSR MANRDHQIRI VDGDTVILAS SLIPGNENAV YRVINGLTRW
GANVVHKGNA KVHVSGHASA GELLYFYNIC RPKNLMPVHG EWRHLRANAE LGALTGVPHD
RIVIAEDGVV VDLIEGKAKI SGKVQAGYVY VDGLSVGDVG EPALKDRKIL GDEGIISVFV
VIDSSTGKIT GGPHVQARGS GIEDSAFGEV IPKITETLER SAQDGVVEPH QMQQLVRRTL
GKWVSDTYRR RPMILPVVVE V
//