ID A0A1H4ADT7_9GAMM Unreviewed; 491 AA.
AC A0A1H4ADT7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-OCT-2025, entry version 28.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN ORFNames=SAMN05660964_01417 {ECO:0000313|EMBL:SEA34046.1};
OS Thiothrix caldifontis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Thiotrichales; Thiotrichaceae; Thiothrix.
OX NCBI_TaxID=525918 {ECO:0000313|EMBL:SEA34046.1, ECO:0000313|Proteomes:UP000199397};
RN [1] {ECO:0000313|EMBL:SEA34046.1, ECO:0000313|Proteomes:UP000199397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21228 {ECO:0000313|EMBL:SEA34046.1,
RC ECO:0000313|Proteomes:UP000199397};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNQP01000006; SEA34046.1; -; Genomic_DNA.
DR RefSeq; WP_093066802.1; NZ_FNQP01000006.1.
DR AlphaFoldDB; A0A1H4ADT7; -.
DR STRING; 525918.SAMN05660964_01417; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000199397; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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; NF008689; PRK11712.1; 1.
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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000199397};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 39..121
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 491 AA; 55425 MW; 15D79FE0CAB2A6BB CRC64;
MSAELLINVT PQESRVALLE NGCLQEVLIE RTSRKGIVGN IYKGKVCRVL PGMEAAFIDI
GLEKSAFLHA SDLTHPSLEE FQSTIPRPTL QISELLYEGK KLLVQVIKDP LGTKGARLTT
HVTIPSRFLV LMPDNNNVGV SGKIEEGSER ERLRGIIEQL RTEFGDEHGY IVRTAAEGIS
EDDLRRDMKF LRKLWESITK TSLESAAPTL VYSDLPLVLR VLRDMVGEKI SKVLIDSRET
ATKVIEFSQK YIPDLASVID HYPGERPIFD LHGVEEEIQK ALQRKVPLKS GGYLIIDQTE
AMTTIDVNTG GFVGSRNLEE TIFRTNLEAA QTIARQLRLR NLGGIIIIDF IDMLQHDHRQ
QVLKLLEKSL ERDYAKTYVC DVSPLGLVEM TRKRTRESLE HILCQPCPCC NGNGFVKSAE
TVCYEVFREI LRAVRQFDAR ELLVLASQEV VDLLLDEESD SLAELQQFVG IPIRLQVESL
YTQEHFDVVL L
//
