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Database: UniProt
Entry: A0A1G1ME81_9BACT
LinkDB: A0A1G1ME81_9BACT
Original site: A0A1G1ME81_9BACT 
ID   A0A1G1ME81_9BACT        Unreviewed;       479 AA.
AC   A0A1G1ME81;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN   ORFNames=A2166_02900 {ECO:0000313|EMBL:OGX15695.1};
OS   Omnitrophica WOR_2 bacterium RBG_13_41_10.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801849 {ECO:0000313|EMBL:OGX15695.1, ECO:0000313|Proteomes:UP000179249};
RN   [1] {ECO:0000313|EMBL:OGX15695.1, ECO:0000313|Proteomes:UP000179249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGX15695.1}.
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DR   EMBL; MHGH01000013; OGX15695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1ME81; -.
DR   STRING; 1801849.A2166_02900; -.
DR   Proteomes; UP000179249; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:SF1; RIBONUCLEASE E_G-LIKE PROTEIN, CHLOROPLASTIC; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   Pfam; PF20833; RNase_E_G_Thio; 1.
DR   Pfam; PF00575; S1; 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   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          39..102
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   479 AA;  55441 MW;  96279DFD8FC63A24 CRC64;
     MPREILINIE TQEKRVAITS DGRLEEFYIE RPQDKTIVGN IYKGKIEAVL PSLGAAFVDI
     GLAKKGFLYL SELESLYEAL EPKEVKSREV KKGQEVMVQV VKESFGTKGP RISCHIGLPG
     RYLVLMPQDN QIGISRRIED EEERRRLRQV LSELKLPKNL GFIVRTAASG RSRNELLRDA
     RFLLKLWQRT EKISQRKQSP ALIYEEYDLT LRAIRDSFTE DVHKLIIDSK PEFYRVQRFM
     KTFLRYLANK VELYRGQDLF EDKDIERQIN KIFENKVYFK SKGYIVIEPT EGLVVIDVNS
     GGFRSKAGHE DAAFKVNCEA AEEVARQLRL RDLGGIIVID FIDMEKEGHR REVLNVLKKA
     LNEDKAKYDI TGISEFGLVE MTRERVHNTV QTLSYESCPY CQGRGKVKSK TTLAIFVLRQ
     LKRFLKTKNM REVTVYLHPS VIEEISKNSQ NLKGLERQFR ARIHLVAEPA CHIEEIKIS
//
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