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Database: UniProt
Entry: A0A259UWN3_9FIRM
LinkDB: A0A259UWN3_9FIRM
Original site: A0A259UWN3_9FIRM 
ID   A0A259UWN3_9FIRM        Unreviewed;       478 AA.
AC   A0A259UWN3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN   Name=rng {ECO:0000313|EMBL:OZC22519.1};
GN   ORFNames=SPACI_13570 {ECO:0000313|EMBL:OZC22519.1};
OS   Sporomusa acidovorans DSM 3132.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa.
OX   NCBI_TaxID=1123286 {ECO:0000313|EMBL:OZC22519.1, ECO:0000313|Proteomes:UP000216052};
RN   [1] {ECO:0000313|EMBL:OZC22519.1, ECO:0000313|Proteomes:UP000216052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3132 {ECO:0000313|EMBL:OZC22519.1,
RC   ECO:0000313|Proteomes:UP000216052};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Sporomusa acidovorans DSM 3132.";
RL   Submitted (FEB-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:OZC22519.1}.
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DR   EMBL; LSLL01000039; OZC22519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259UWN3; -.
DR   STRING; 112900.SAMN04488499_102022; -.
DR   Proteomes; UP000216052; 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, ECO:0000313|EMBL:OZC22519.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216052};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          39..111
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   478 AA;  53551 MW;  8E96AA7F783C9928 CRC64;
     MNKSIITNVM PEETRVAVLE DGELMEISVE RSESGHLVGN IYKGRVKNVL PGMQAAFIDI
     GRDKNAFLYM GDAGRQAAGR HLTIGQDVLV QIAKDAMGDK GPRATISLTL PGRYIVLMPT
     VDYIGISRRI EDEAERNRLR QLADKIRPDG MGVIVRTVAK GKSQDELMKD MAYLVNMWST
     LSARAKRTSA PALIYKDADL VVRIVRDYLT NDVTQFVIDS QEAYNRVVDL LRYISPELMD
     CVSLFESNAQ SGDVFSRYNL DVALESLQSR RVDLKCGGYL VIDHTEALTV IDVNTGKFVG
     NTNLSETVFQ TNLEATVEIA RQLRLRDIGG IIIIDFIDMD KPEQRAAVLT GLETALKKDR
     TKSNVLGITS LGLVEMTRKK ARQNLSGMLY SPCPHCRGKG RIKSPETVII DIKREVRNLN
     KRSRPGGRLL IQVHPQVADL LKRQDEVRRL EQETARTLAV EPVADMNPER FSLLWKPD
//
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