ID A0A2D0L6X5_9GAMM Unreviewed; 489 AA.
AC A0A2D0L6X5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN ORFNames=Xkoz_02797 {ECO:0000313|EMBL:PHM71400.1};
OS Xenorhabdus kozodoii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351676 {ECO:0000313|EMBL:PHM71400.1, ECO:0000313|Proteomes:UP000221101};
RN [1] {ECO:0000313|EMBL:PHM71400.1, ECO:0000313|Proteomes:UP000221101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17907 {ECO:0000313|EMBL:PHM71400.1,
RC ECO:0000313|Proteomes:UP000221101};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC {ECO:0000256|ARBA:ARBA00005663}.
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:PHM71400.1}.
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DR EMBL; NJCX01000020; PHM71400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D0L6X5; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000221101; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd04453; S1_RNase_E; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR InterPro; IPR004659; RNase_E/G.
DR InterPro; IPR048583; RNase_E_G_thioredoxin-like.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00757; RNaseEG; 1.
DR PANTHER; PTHR30001; RIBONUCLEASE; 1.
DR PANTHER; PTHR30001:SF0; RIBONUCLEASE G; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR Pfam; PF20833; RNase_E_G_Thio; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 39..128
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 489 AA; 55266 MW; DDD6A7FD03EA9D7B CRC64;
MTAELLVNVT PSETRVAYID GGILQEIHIE REAKRGIVGN IYKGRVSRVL PGMQAAFVDI
GLEKAAFLHA SDIVPHTECI AGEERKNFHV RDIAELVRQG QDLLVQVVKD PLGTKGARLT
TDITLPSRYL VFMPGASHVG VSQRIESEEE RERLKSIVMA YCDEEGGFII RTAAEGVGAE
ELAQDAAFLK RLWSKVIERK KRNITKYKVY GELALAQRVL RDFVGASLDR IRVDSRQTFI
QLQEFIDEYI PEMNAKLEHY QGNQPIFDLF DVENEIQRAL ERKVELKSGG YLIIDQTEAM
TTIDINTGAF VGHRNLEETI FNTNIEAAQA IARQLRLRNL GGIIIIDFID MGNEEHRRRV
LASLEQALSK DRVKTTLNGF SQLGLVEMTR KRTRESIEHI LCDNCPTCQG RGTVKSVETV
CYEVLREIVR VNRAIDADRF LVYASPAVSE TLKGDESHAL AEVEIFVGKQ VKVQTEQRYS
QEQFDVIMM
//
