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Database: UniProt
Entry: A0A0F6AD18_9GAMM
LinkDB: A0A0F6AD18_9GAMM
Original site: A0A0F6AD18_9GAMM 
ID   A0A0F6AD18_9GAMM        Unreviewed;       490 AA.
AC   A0A0F6AD18;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Ribonuclease G {ECO:0000256|ARBA:ARBA00017719};
GN   ORFNames=N479_11735 {ECO:0000313|EMBL:KKE84075.1};
OS   Pseudoalteromonas luteoviolacea S4054.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE84075.1, ECO:0000313|Proteomes:UP000033434};
RN   [1] {ECO:0000313|EMBL:KKE84075.1, ECO:0000313|Proteomes:UP000033434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4054 {ECO:0000313|EMBL:KKE84075.1,
RC   ECO:0000313|Proteomes:UP000033434};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KKE84075.1}.
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DR   EMBL; AUXW01000139; KKE84075.1; -; Genomic_DNA.
DR   RefSeq; WP_046355800.1; NZ_AUXW01000139.1.
DR   AlphaFoldDB; A0A0F6AD18; -.
DR   PATRIC; fig|1129367.4.peg.2139; -.
DR   Proteomes; UP000033434; Unassembled WGS sequence.
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   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          39..123
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   490 AA;  55119 MW;  2822C7553FF0D831 CRC64;
     MSSELLINVT PSESRVALIE NGVLQEVQVE RVGNLGIVGN IYLGKVSRVL PGMQAAFVDI
     GLEKAAFLHA SDIVSSASIE EAVDDQPIKK VQDIRELVKQ GQFIMVQVVK DPIGTKGARL
     TTDITIPSRY LVFMPDATHV GVSQRIETEE ERDRLKHIVA EYNDENGGFI VRTAAEGAAE
     AELKHDAEFL KKLWQKIINK RRKTSKASIL HEDLTLAFRT LRDYVGEDME RIRVDSKLTY
     QQLKTFTEEF VPQLSETLEY YPGERPIFDL FDVEAEIQKA LHRKVELKSG GYLIIDQTEA
     MTTVDVNTGA FVGHRNLEET IFNTNVEATS AIARQLRLRN LGGIIIIDFI DMVSDEHKRR
     VLHSLEAALA KDRAKANING LSALGLVEMT RKRTRESLEH ILCDVCPSCS GRGSLKTVET
     VCYEILREIV RVNRAYEADK FMVYASAAVS EALVNDEYHN LAELELFIGK QVSIQTENLY
     SQEQFDVVMM
//
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