ID A0A1H3S8S9_9FIRM Unreviewed; 498 AA.
AC A0A1H3S8S9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN ORFNames=SAMN05660462_02774 {ECO:0000313|EMBL:SDZ34294.1};
OS Proteiniborus ethanoligenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX NCBI_TaxID=415015 {ECO:0000313|EMBL:SDZ34294.1, ECO:0000313|Proteomes:UP000198625};
RN [1] {ECO:0000313|EMBL:SDZ34294.1, ECO:0000313|Proteomes:UP000198625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21650 {ECO:0000313|EMBL:SDZ34294.1,
RC ECO:0000313|Proteomes:UP000198625};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNQE01000039; SDZ34294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3S8S9; -.
DR STRING; 415015.SAMN05660462_02774; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000198625; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000198625};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 38..106
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 498 AA; 56941 MW; 341B90D838E975CC CRC64;
MNQIIIDVGI QENRVAVIEN NELVEIYIEK DDNKRIVGNI YKGRVVNVLP GMQAAFVDIG
LEKNAFLYVK DAIPKEMLSN KKLNLKDISI KDVIKSGQDI IVQVIKEPFG SKGARVTTHI
TIPGRHIVLM PYTDYIGISR RISNETERNR LKEIAESIKP ENMGLILRTA VEGLGIEDFK
DDIKFLLKVL NKIDSERNLG FAPRVMYKDL DLVHRTVRDL FTNNVEKLVI NNRDEYKSIV
ELVEMISPQL KSRVEYFDLS YDIFGHFGIS QDMNKALDRK VWLKSGGYVI IDETEALTSI
DVNTGKYVGT INLEDTVLKT NIEAAKEIAK QVRLRNIGGI IIIDFIDMNN EEHEKEVLEI
LKNELKKDRT KSTVLGITQL GLVEMTRKKV RSRLTSHLLK ECPYCDGTGR VYSEGFVIGL
IEKEIKRLKL HTSAEAVILE VNPHIAKYLY DNNNYIIRRI EGEYGINMFI RESDSIHHNE
IKVKNIGKVD FIKGILDK
//
