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Database: UniProt
Entry: J4V095_9GAMM
LinkDB: J4V095_9GAMM
Original site: J4V095_9GAMM 
ID   J4V095_9GAMM            Unreviewed;       666 AA.
AC   J4V095;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN   ORFNames=NT01SARS_0533 {ECO:0000313|EMBL:EJP72047.1};
OS   SAR86 cluster bacterium SAR86A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX   NCBI_TaxID=1123866 {ECO:0000313|EMBL:EJP72047.1, ECO:0000313|Proteomes:UP000010305};
RN   [1] {ECO:0000313|EMBL:EJP72047.1, ECO:0000313|Proteomes:UP000010305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22170421; DOI=10.1038/ismej.2011.189;
RA   Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., Valas R.,
RA   Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., Halpern A.L.,
RA   Lasken R.S., Nealson K., Friedman R., Venter J.C.;
RT   "Genomic insights to SAR86, an abundant and uncultivated marine bacterial
RT   lineage.";
RL   ISME J. 6:1186-1199(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; JH611156; EJP72047.1; -; Genomic_DNA.
DR   AlphaFoldDB; J4V095; -.
DR   STRING; 1123866.NT01SARS_0533; -.
DR   HOGENOM; CLU_003468_5_3_6; -.
DR   Proteomes; UP000010305; 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:UP000010305};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          39..115
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          487..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..571
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..666
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   666 AA;  75780 MW;  91C2463F9452881B CRC64;
     MKRILINSSY GDELRVALVD GAKLYDFDTE SPERTLLKGS IYKATVSRIE SSLDAAFVNF
     GSDRHGFLPL KDLSKEFYKK DKKGKYVCTL EEGQEIIVQV TKEERGTKGA ALTTQIGLAG
     RFLVLIPNST RSGGISRRIS GDERDQIKAA LEKLNIPENM SAIVRTNGLG RTVEELSLDL
     SYLLALWEEI NNTTPNATSP SLIFRDDKLI VRVVRDYFKE DIEEILIDDK DIFTEAKEFI
     EAVIPDHSDK VKFYDEDIPL FNRYQIESQI ELAFQREISL NSGGSIVIDP TEAMTTIDVN
     SARSTKGKDI EETAFKTNLE AASEIARQLR LRDVGGLVVI DFIDMTDEDN QNKVESAFRK
     AVYSDRARVQ FSGISRFGLL EVSRQRLRPS LNESYDIEHV LVRGPRSLGQ SILRIVGEDA
     AKDNTGEIQV YVPADVASYL LNEKRYDIIN IEKTNNIKVL IIADPYKTRP YYKVVRVKKS
     DVKDISSYAL TPSSPEPDTN WRDNKNSSKN VKPLVDGVKP PKMPKRRKAG IVKWLKTITG
     IEVDEKTSKK KSIKRRPRRK PQNKQKNNSK ARKNYQKNNE NVKTKTNKKP VSKKQQNQKK
     SKQKDFNKND NKNVSKDIEN TKSVKKNNEQ LNVDDKKKSP IKEIVKEKKV KKEIPTRAKN
     DPRQTS
//
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