ID A0A291P5K7_9GAMM Unreviewed; 487 AA.
AC A0A291P5K7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN Name=rng {ECO:0000313|EMBL:ATJ82148.1};
GN ORFNames=BEI_1161 {ECO:0000313|EMBL:ATJ82148.1};
OS Halomonas beimenensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=475662 {ECO:0000313|EMBL:ATJ82148.1, ECO:0000313|Proteomes:UP000219993};
RN [1] {ECO:0000313|EMBL:ATJ82148.1, ECO:0000313|Proteomes:UP000219993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTU-111 {ECO:0000313|EMBL:ATJ82148.1,
RC ECO:0000313|Proteomes:UP000219993};
RX PubMed=29026163;
RA Chen Y.H., Lin S.S., Shyu Y.T.;
RT "Revealing the Saline Adaptation Strategies of the Halophilic Bacterium
RT Halomonas beimenensis through High-throughput Omics and Transposon
RT Mutagenesis Approaches.";
RL Sci. Rep. 7:13037-13037(2017).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP021435; ATJ82148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291P5K7; -.
DR KEGG; hbe:BEI_1161; -.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000219993; 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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000219993};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 39..115
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 487 AA; 54838 MW; 1F55EA6098C65C7F CRC64;
MSGEVLINLT PMETRVAVVE NGVLQEAFIE RARRRGIVGN IYKGKVVRVL PGMQAAFVDI
GLDRAAFIHA HEVMPPGTPA DEQVSIAQLL HEGQSLVVQV TKDPIGSKGA RLTTHLSVPS
RYLVYMPDSP HNGVSQRIED EGERERLRDL VEAAQAEQTL EVTGGFIVRT AAEGVSLEEM
VGDMHFLLRL WRKVSERKIS APAPSVIYDD LPLFMRTLRD VMRDDIEKVR IDSRENYVKL
VEFAEEFMPS AVERIEHYAG ERPIFDLFSV EDEIQKALGR KVQLKSGGYL VIDPTEAMTT
IDVNTGGFVG HRNLEETIFK TNLEAATAIA RQLRLRNLGG IIIIDFIDME DPEHQRQVLR
VLEKALERDH AKTKCTGVTE LGLVQVTRKR TRESLEQTLC EACPACQGRG TLKTPESVCY
EIFREILREE RAYSAETYTV LASQSVVDRL LDEESAAVAD LEEFIGKTIR FQVESHYSQE
QYDIVLM
//
