ID D4GL30_PANAM Unreviewed; 130 AA.
AC D4GL30;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 28-JAN-2026, entry version 46.
DE RecName: Full=Endoribonuclease SymE {ECO:0000256|HAMAP-Rule:MF_01193};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01193};
GN Name=yjiW {ECO:0000313|EMBL:ADD76076.1};
GN Synonyms=symE {ECO:0000256|HAMAP-Rule:MF_01193};
GN OrderedLocusNames=PANA_0909 {ECO:0000313|EMBL:ADD76076.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD76076.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD76076.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD76076.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
CC -!- FUNCTION: Involved in the degradation and recycling of damaged RNA. It
CC is itself a target for degradation by the ATP-dependent protease Lon.
CC {ECO:0000256|HAMAP-Rule:MF_01193}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01193}.
CC -!- SIMILARITY: Belongs to the SymE family. {ECO:0000256|HAMAP-
CC Rule:MF_01193}.
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DR EMBL; CP001875; ADD76076.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GL30; -.
DR STRING; 706191.PANA_0909; -.
DR KEGG; pam:PANA_0909; -.
DR eggNOG; ENOG5031VID; Bacteria.
DR HOGENOM; CLU_151239_0_0_6; -.
DR Proteomes; UP000001702; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR HAMAP; MF_01193; Endoribonucl_SymE; 1.
DR InterPro; IPR014944; Toxin_SymE-like.
DR InterPro; IPR020883; TypeI_TA_SymE.
DR NCBIfam; NF010128; PRK13605.1; 1.
DR Pfam; PF08845; SymE_toxin; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01193};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01193};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01193};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01193};
KW Reference proteome {ECO:0000313|Proteomes:UP000001702};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01193}.
FT DOMAIN 22..72
FT /note="Toxin SymE-like"
FT /evidence="ECO:0000259|Pfam:PF08845"
SQ SEQUENCE 130 AA; 14871 MW; FEECB6C43FDD45D6 CRC64;
MIMAEHDTKP EVATAEAPEL KNRRYTVGYI HNWKTHNKVT AITLKGDWLA DACFETGRPL
KVRMMPGCLA LTAQEPQPSE PEIMQMLKKV CKLSARKQKQ IVEFITVIAT PQKRPLPLGT
VVWEDMSRRR
//
