ID I0HVZ9_RUBGI Unreviewed; 486 AA.
AC I0HVZ9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN Name=cafA {ECO:0000313|EMBL:BAL97186.1};
GN Synonyms=rng {ECO:0000313|EMBL:BAL97186.1};
GN OrderedLocusNames=RGE_38470 {ECO:0000313|EMBL:BAL97186.1};
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL97186.1, ECO:0000313|Proteomes:UP000007883};
RN [1] {ECO:0000313|EMBL:BAL97186.1, ECO:0000313|Proteomes:UP000007883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX PubMed=22689232; DOI=10.1128/JB.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.P.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(2012).
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; AP012320; BAL97186.1; -; Genomic_DNA.
DR RefSeq; WP_014430037.1; NC_017075.1.
DR AlphaFoldDB; I0HVZ9; -.
DR STRING; 983917.RGE_38470; -.
DR KEGG; rge:RGE_38470; -.
DR PATRIC; fig|983917.3.peg.3756; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_4; -.
DR Proteomes; UP000007883; 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, ECO:0000313|EMBL:BAL97186.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007883};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 40..118
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 486 AA; 53815 MW; FE399FEE0AA8CEE6 CRC64;
MATQDILINW APQETRVAIV ENGAVQELHV ERTLERGLVG NVYLGKVARV LPGMQSAFVD
IGLERAAFLH VADLFGHPTT RGDAPLPPIE RHVFEGQTLT VQVIKDAIGT KGARLSTQIS
IAGRMLVFLP HDDHIGISQK IGGPELREQL RTRMQALAGS EGGGFILRTN AEEASDAELA
DDIAYLRKAW AAIRQRAQSK PPGTLLHQDL SLAERVLRDL TSDATQTLRI DSKLQYEALR
AFGESYTPGA VRKLELYRGE RPIFDLFNIE EEIAKALARR VDLKSGGYLI IDQTEALTTI
DVNTGGFVGA RNFEDTIFKT NLEAAGAIAR QLRLRNLGGI IIADFIDMTR DEHQQAVLAE
LRKQLARDRT RTTVSGFTQL GLVEMTRKRT RESLAHMLCE PCPTCQGRGQ VKTARSVCYD
ILREILREAR QFNPKEFRVI ASAAVVEMLL DEESGHIAGL SEFIGKPISL SAEATMNPEQ
YDIVLM
//
