ID A0A1B7LH96_9FIRM Unreviewed; 562 AA.
AC A0A1B7LH96;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN ORFNames=A6M21_05475 {ECO:0000313|EMBL:OAT85571.1};
OS Desulfotomaculum copahuensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1838280 {ECO:0000313|EMBL:OAT85571.1, ECO:0000313|Proteomes:UP000078532};
RN [1] {ECO:0000313|EMBL:OAT85571.1, ECO:0000313|Proteomes:UP000078532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMa1 {ECO:0000313|EMBL:OAT85571.1,
RC ECO:0000313|Proteomes:UP000078532};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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:OAT85571.1}.
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DR EMBL; LYVF01000054; OAT85571.1; -; Genomic_DNA.
DR RefSeq; WP_066666709.1; NZ_LYVF01000054.1.
DR AlphaFoldDB; A0A1B7LH96; -.
DR STRING; 1838280.A6M21_05475; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000078532; 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-UniRule.
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; 2.
DR Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 1.
DR InterPro; IPR004087; KH_dom.
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 InterPro; IPR002792; TRAM_dom.
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 Pfam; PF01938; TRAM; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 2.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
DR PROSITE; PS50926; TRAM; 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:UP000078532};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117}.
FT DOMAIN 39..127
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 499..561
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
SQ SEQUENCE 562 AA; 63243 MW; A12CB403FC7EEA98 CRC64;
MFKEIVINAG DEETRAAVLE DRVLVEMYIE RSANQRLVGN IFHGRVENVL PGMQAAFVDI
GLEKNAFLYV EDALPPRSPD NHHHGGALGG NIGDILKRGQ EVIVQIVKEP IGTKGPRVTT
HITLPGRYVV LMPTMDYIGI SRRIDSEKER DRLKELAGRF KPHGMGMIVR TVAEGVDDEE
LRQDIQLLSK LWRKILQRGS HGPVPNLIHR DLELIQRILR DVFTEDVDRL TVDSRYEYEK
IMELLDITGP RLKFKVFLEE RDNIFQDYGI EQELEKALKR KVWLKCGGYM IIDQAEALTA
VDVNTGKFVG STNLEDTVLR TNLDAAVEIA RQLRLRNIGG IIVVDFIDMQ KEENRRQVLH
VLEEEIKKDK TKANILGITG LGLVEMTRKK VRPSLSEVLQ RPCPYCEGRG KVLSEETVGI
HFKNHIIELA RRTSADTILV EANPLVAARL IGSGGSNLRE LEQKTGKNVY IRGSQGQHIE
SVNVRPLHDS EEIRAHTLPV KPGQVLEVRV EEPHVSNTND GIARIDGFIL DIEGAGALVG
EKVPVEVSKV FRTYARAKLV KS
//
