ID D9SD74_GALCS Unreviewed; 484 AA.
AC D9SD74;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN OrderedLocusNames=Galf_2676 {ECO:0000313|EMBL:ADL56672.1};
OS Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS capsiferriformans (strain ES-2)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Gallionella.
OX NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL56672.1, ECO:0000313|Proteomes:UP000001235};
RN [1] {ECO:0000313|EMBL:ADL56672.1, ECO:0000313|Proteomes:UP000001235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-2 {ECO:0000313|EMBL:ADL56672.1,
RC ECO:0000313|Proteomes:UP000001235};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Shelobolina E.S., Picardal F., Roden E., Emerson D.,
RA Woyke T.;
RT "Complete sequence of Gallionella capsiferriformans ES-2.";
RL Submitted (AUG-2010) 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; CP002159; ADL56672.1; -; Genomic_DNA.
DR RefSeq; WP_013294591.1; NC_014394.1.
DR AlphaFoldDB; D9SD74; -.
DR STRING; 395494.Galf_2676; -.
DR KEGG; gca:Galf_2676; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_4; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000001235; Chromosome.
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:UP000001235};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 39..115
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 484 AA; 54694 MW; 6BE7168867FC77E3 CRC64;
MSEEILINVT PQETRVAVMQ LGVVQELHIE RGSNRGIAGN VYLGRIKRVL PGMQSAFIDI
GLERSAFLHV ADIWENSNSG IEAKPIEKIL FEGQNLLVQV IKEPIGSKGA RLTTQLSFAG
RLLVFLPQEM RIGVSQRIEG TEQRDALRAK LQAILPPDHH GGYIIRTVAE AKDDAHFAID
IAYLDKLWSN LQTAAKTASA PQLLYQELDI SLRVLRDFVS EETARILIDS RSTRNKMLEF
ADNYNADAAQ LLEHYTGARP LFDMYNIEEE IERALSKRVD LKSGGYLIID QTEALTTVDV
NTGGFVGVRN FDDTIFKTNL EATQVIARQL RLRNLGGIII CDFIDMDNLQ HRDAVLEEFK
KALARDHTRI SVNNFSSLGL VEMTRKRTRE SLAHVLCEPC PTCKGRGEVK TAQTVCYEIL
REIVREARQF DAREYRILAS QQVIDLFLEE ESQALAGLSD FIEKPISMLV ENQYNQEQYD
VILM
//
