ID A0A1G7QAD9_9BURK Unreviewed; 488 AA.
AC A0A1G7QAD9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN ORFNames=SAMN05216320_102125 {ECO:0000313|EMBL:SDF94550.1};
OS Duganella sp. OV458.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1855290 {ECO:0000313|EMBL:SDF94550.1, ECO:0000313|Proteomes:UP000199454};
RN [1] {ECO:0000313|EMBL:SDF94550.1, ECO:0000313|Proteomes:UP000199454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV458 {ECO:0000313|EMBL:SDF94550.1,
RC ECO:0000313|Proteomes:UP000199454};
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; FNCD01000002; SDF94550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7QAD9; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000199454; 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 RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 39..119
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 488 AA; 54606 MW; 57EA70A0F5B9924E CRC64;
MNEDILINIT PQETRVALIM QGAVQELHIE RTLTRGLAGN VYSGKVVRVL PGMQSAFIDI
GLERAAFLHV ADIWEARPHD GGSNATPTPI EKLLFDGQVL TVQVIKDPIG TKGARLSTQI
SIAGRMLVYL PQDGHIGVSQ KIEKESEREA LRTRLQSLLP KEEKGGYIIR TQAEDASDAD
IAGDVEYLRK TWAAITHGAR TRPATTLLHQ DLSLAQRVLR DFVHEETATI QVDSRENYVN
LQEFGQAYTP GVLPRLHHYT GERPLFDLYG VEEEILRALG RRVDLKSGGY LIVDQTEAMT
TIDVNTGGFV GGRNFADTIF KTNLEAAHAI ARQLRLRNLG GIIILDFIDM ENTEHRTAVL
GELKKALSRD RTKVSVSSFS ALGLVEMTRK RTRESLAHIL CEPCPACNGK GQVKTSRTIC
YEILRELLRE AKQFNPREFR ILASQEVVDM FLEEESQHLA MLGDFIGKKI SLQVETAYHQ
EQYDVILM
//
