ID S7VK30_DESML Unreviewed; 514 AA.
AC S7VK30;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN ORFNames=dsmv_0959 {ECO:0000313|EMBL:EPR44923.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR44923.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR44923.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR44923.1,
RC ECO:0000313|Proteomes:UP000014977};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
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:EPR44923.1}.
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DR EMBL; ATHJ01000011; EPR44923.1; -; Genomic_DNA.
DR AlphaFoldDB; S7VK30; -.
DR STRING; 897.B2D07_11685; -.
DR PATRIC; fig|1121405.3.peg.115; -.
DR eggNOG; COG1530; Bacteria.
DR Proteomes; UP000014977; 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 Reference proteome {ECO:0000313|Proteomes:UP000014977};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 68..146
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 514 AA; 58507 MW; 640246CB13C3128F CRC64;
MSTKEVAVKI TIRKSIQFIF EKGQTPRHMS SKILINAVDH DECRIAKVTD SKLEEFNIEN
AAREITHGNI YKGIITRIEP GLQSVFVDYG AERHGFLQKH EIHSDYFQDN RTGEDSISNL
VRRGQELLVQ VTKDPILNKG AMLTTFISLP GRYIVLMPGS KNKGISRKIE DEEERNRLKE
LLGMLKIPDG FGLIIRTAGA SCTKTRLAKD LRYLLTLWKN INKKGIGESA PALLYKERHL
VLRSIRDSFT HDVKEILVDT ESVYQEIKDF IHIISPKHTR IVKLYKGDKP IFTKYELEDQ
IASIYENRVD LKSGGSIVID PTEALVAIDV NSGKSTQKRS IEQTAFSTNI EAAEEIARQL
RLRDLGGLIV IDFIDMRESK HKLEVERNLK SFIKLDKARI KVGRISRFGL LEMSRQRIRP
SIEFGNFQPC KYCGGKGQLP STEMLGLNIL RRLQLETLKQ GITRVKGVVP LDVADYLLNK
KRREILDLEV RRDISILIEG DAAMLPKEST ITSE
//
