ID A0A1E7RLM4_9GAMM Unreviewed; 495 AA.
AC A0A1E7RLM4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN ORFNames=BIY45_12560 {ECO:0000313|EMBL:OEZ00275.1};
OS Stenotrophomonas sp. BIIR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=1904462 {ECO:0000313|EMBL:OEZ00275.1, ECO:0000313|Proteomes:UP000175905};
RN [1] {ECO:0000313|EMBL:OEZ00275.1, ECO:0000313|Proteomes:UP000175905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIIR7 {ECO:0000313|EMBL:OEZ00275.1,
RC ECO:0000313|Proteomes:UP000175905};
RA Sanchez-Castro I., Ruiz-Fresneda M.A., Bakkali M., Kampfer P., Busse H.J.,
RA Lopez-Fernandez M., Martinez-Rodriguez P., Merroun M.L.;
RT "Stenotrophomonas bentonitica sp. nov., isolated from bentonite
RT formations.";
RL Submitted (SEP-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}.
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:OEZ00275.1}.
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DR EMBL; MKCZ01000055; OEZ00275.1; -; Genomic_DNA.
DR RefSeq; WP_070208402.1; NZ_MKCZ01000055.1.
DR AlphaFoldDB; A0A1E7RLM4; -.
DR STRING; 1904462.BIY45_12560; -.
DR GeneID; 84659852; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000175905; 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:UP000175905};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 39..126
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 495 AA; 55254 MW; 74BD5AB67FF89F9C CRC64;
MSEEILVNVT PRETRVAVIE NGMLQELHIE RGWRRGVVGN IYKGKVQRVM PGMQAAFVEV
GLERAAFLHA NDVVRPAPVA SADTEGTTLP PPSSVPIVEL LRDGQDIVVQ VVKDPIGTKG
ARLTTQISIP SRYMVLLPQS KVVGVSARIE DEAERARLKT LVTELSAQHG GYGYIVRTNA
EGQPAEAIAE DIAYLSRVWN VVERRGREAA PCSVIYEDLS LPLRSVRDLI RKDVDKVKVD
SKETFTQLQA FVAKYMPVLA EKLELYSGDR PIFDMFGVED EIGRALDKQV PLKSGGYLVI
DQTEAMTTID VNTGSFLGQR NLEETVFRTN LEAAQSVARQ LRLRNLGGII IIDFIDMDDA
EHRRQVLRTL EKALARDHAK TTVYEFSPLG LVEMTRKRTV ESLERQLSEP CPECSGRGSI
KTAETVTYEI FREITRAVRQ FDAARLLVIA SSKVVARITD EESAAVAELE EFLGKSIRFQ
ADEQYLQEQF DVVLL
//
