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Database: UniProt
Entry: A0A1I1R203_9GAMM
LinkDB: A0A1I1R203_9GAMM
Original site: A0A1I1R203_9GAMM 
ID   A0A1I1R203_9GAMM        Unreviewed;       487 AA.
AC   A0A1I1R203;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN   ORFNames=SAMN05660831_01323 {ECO:0000313|EMBL:SFD26148.1};
OS   Thiohalospira halophila DSM 15071.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalospirales;
OC   Thiohalospiraceae; Thiohalospira.
OX   NCBI_TaxID=1123397 {ECO:0000313|EMBL:SFD26148.1, ECO:0000313|Proteomes:UP000198611};
RN   [1] {ECO:0000313|EMBL:SFD26148.1, ECO:0000313|Proteomes:UP000198611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL3 {ECO:0000313|EMBL:SFD26148.1,
RC   ECO:0000313|Proteomes:UP000198611};
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; FOMJ01000003; SFD26148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1R203; -.
DR   STRING; 1123397.SAMN05660831_01323; -.
DR   OrthoDB; 9804278at2; -.
DR   Proteomes; UP000198611; 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};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198611};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          39..118
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   487 AA;  54464 MW;  88DE330A4D2923E7 CRC64;
     MSEELLINVT PHETRVAMVE NGVLQEVRIE RSTGRGLVGN IYKGKVVRVL PGMQSAFVEV
     GLARTAFLHA SDVAVGEGEG RRNGNEQDIR ALLREGQEIL VQVVKDPIGG KGARLTTHLT
     IPSRYLVFLP GGHHVGISQK IEDAEERERL RAMVAAASEG EERGGYIVRT VAEGAGEAEV
     AADVTYLQRL WDSIHDRAAA TTAPGLVHED LPLALQVLRD MAGTPYERVR VDSRETYQRI
     REFAETFVPE MVELIEHYPG ERPLFDLYSV EEEIQKALER KVELKSGGYL VIDQTEAMTT
     VDVNTGAYVG HRNLEETIFK TNLEAAQAIA RQLRLRNLGG IIILDFIDMG DQEHRRQVLR
     ALESALERDR ARARICEVSA LGLVEMTRKR TRESLEQILC EPCPTCGGRG SVKTTATVCY
     EIFREVLRSA RQFDTRELLV LAAQEVVDRM LDEESASVAE LEDFIGRSVR FQVEALYTQE
     QFDVVLL
//
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