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Database: UniProt
Entry: A0A0W0WKX3_9GAMM
LinkDB: A0A0W0WKX3_9GAMM
Original site: A0A0W0WKX3_9GAMM 
ID   A0A0W0WKX3_9GAMM        Unreviewed;       649 AA.
AC   A0A0W0WKX3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN   ORFNames=Lnau_2616 {ECO:0000313|EMBL:KTD32968.1};
OS   Legionella nautarum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD32968.1, ECO:0000313|Proteomes:UP000054725};
RN   [1] {ECO:0000313|EMBL:KTD32968.1, ECO:0000313|Proteomes:UP000054725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD32968.1,
RC   ECO:0000313|Proteomes:UP000054725};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) 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}.
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:KTD32968.1}.
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DR   EMBL; LNYO01000024; KTD32968.1; -; Genomic_DNA.
DR   RefSeq; WP_058505601.1; NZ_LNYO01000024.1.
DR   AlphaFoldDB; A0A0W0WKX3; -.
DR   STRING; 45070.Lnau_2616; -.
DR   PATRIC; fig|45070.6.peg.2762; -.
DR   OrthoDB; 9804278at2; -.
DR   Proteomes; UP000054725; 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   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          39..121
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          515..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   649 AA;  73173 MW;  71485483FA406E42 CRC64;
     MEKMLINATQ TEEVRVALVK DNDLYDLDIE CPSEVKKKGN IYKALVTRRE PSLDAVFVEY
     GAKRQGFLPL KEIAPEYLSK HPDDFGDEKP PITSLIREGQ ELLIQVDKEE RGNKGAALTT
     YITLAGCYLV LMPNNPNSGG ISRRIEGDDR DELKETLNAL QLPDGMGLII RTAGVGKNIE
     ELQADLDMLC NQWQAIRQAY NTQLAPCLIH QEGDVIIRSI RDNLRKSIGE IIIDDQISYV
     KAKQYIEQVK PDFLPNLKLY NNTIPLFNFY QIESQIETAY QREVLLPSGG ALVIDRTEAL
     ISIDINSAKA TSGSDIETTA LNTNLEAADE IARQLRLRDL GGLVVIDFID MSSSKNQRDV
     ENRLKEALKA DRARIQVGRI SRFGLLEMSR QRLRLSLGEN AQEVCPRCEG RGTVRNIQSH
     GLSITRLIEE EALKEKTAEV QVQLPVELAT FIINEKREFI LNIEKRHNVH VLIIANPYMH
     PPQYNIIRLK EDNVGKNKKP SYTLIQQPEL NVVRADQEAT KHDEPAVKGF SGHQPAKTQH
     NSFIKRLWSS LFGSISEAST TSTPITATPS RQERSSRSTQ QPQRQTNQSA SGEKRQSNQP
     NRRRRPGNQQ RNTSGNPQRR RSQPGQQSAG RVVPLKPDSN KKKESANKE
//
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