ID A0A0Q7LD62_9BURK Unreviewed; 508 AA.
AC A0A0Q7LD62;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN ORFNames=ASD34_14495 {ECO:0000313|EMBL:KQX87490.1};
OS Variovorax sp. Root473.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1736541 {ECO:0000313|EMBL:KQX87490.1, ECO:0000313|Proteomes:UP000051275};
RN [1] {ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|Proteomes:UP000051275};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX87490.1, ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|EMBL:KQX87490.1,
RC ECO:0000313|Proteomes:UP000051275};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQX87490.1}.
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DR EMBL; LMEV01000017; KQX87490.1; -; Genomic_DNA.
DR RefSeq; WP_056580445.1; NZ_LMEV01000017.1.
DR AlphaFoldDB; A0A0Q7LD62; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000051275; 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.
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:UP000051275};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 36..129
FT /note="S1 motif"
FT /evidence="ECO:0000259|SMART:SM00316"
SQ SEQUENCE 508 AA; 56352 MW; 2BF817D34E5799B9 CRC64;
MQDILINWSP QETRVALVEH GAVQELHVER TLERGLVGNI YLGKVSRVLP GMQSAFIDIG
LERTAFLHVA DIVSPFTPGS RPSATPPERD HRNGGPMVPI EKQVFEGQSL LVQVIKDPIG
TKGARLSTQI SIAGRLLVFL PQDNHIGVSQ KIPPDQRESL RNRMLALIEA AAAAESGGVV
PVNTGGFILR TNGEDAADAE LAEDIAYLRK TWTRIREASS RMPAMSLLHQ DLSLLQRVLR
DMTSEDTQTI RIDSREQFEV LLKFGLEFMP QAAGKLQHYK GERPIFDLYS VDEEIAKALG
RRVDLKSGGY LVVDQTEALT TVDVNTGGFV GARNFDDTIF KTNLEAAQAI ARQLRLRNLG
GIIIVDFIDM ARDDHREQVL AEFRKQLARD RVKTTAGGFS QLGLVEMTRK RTRESLAHML
CEPCVACGGQ GIVKTARSVA YDVMREILRE ARQFTPREFR IVSSPQVIEL FLDEESQHLA
GLSDFIGKPI SLQSEPAIGQ GQYDIVLL
//
