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Database: UniProt
Entry: F3GEQ1_PSESJ
LinkDB: F3GEQ1_PSESJ
Original site: F3GEQ1_PSESJ 
ID   F3GEQ1_PSESJ            Unreviewed;       132 AA.
AC   F3GEQ1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=NUDIX hydrolase {ECO:0000313|EMBL:EGH45551.1};
GN   ORFNames=PSYPI_25909 {ECO:0000313|EMBL:EGH45551.1};
OS   Pseudomonas syringae pv. pisi str. 1704B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH45551.1, ECO:0000313|Proteomes:UP000004986};
RN   [1] {ECO:0000313|EMBL:EGH45551.1, ECO:0000313|Proteomes:UP000004986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1704B {ECO:0000313|EMBL:EGH45551.1,
RC   ECO:0000313|Proteomes:UP000004986};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC       {ECO:0000256|ARBA:ARBA00005582, ECO:0000256|RuleBase:RU003476}.
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:EGH45551.1}.
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DR   EMBL; AEAI01001332; EGH45551.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3GEQ1; -.
DR   PATRIC; fig|629263.4.peg.4195; -.
DR   HOGENOM; CLU_037162_25_1_6; -.
DR   BioCyc; PSYR629263:G11X0-4568-MONOMER; -.
DR   Proteomes; UP000004986; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd04667; Nudix_Hydrolase_10; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR43736; ADP-RIBOSE PYROPHOSPHATASE; 1.
DR   PANTHER; PTHR43736:SF1; ADP-RIBOSE PYROPHOSPHATASE; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003476}.
FT   DOMAIN          1..118
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   132 AA;  14366 MW;  35EB737B1AA9CFFE CRC64;
     MKQRATVICK RDGQVLYVRK PKSRWALPGG KIEAGETPFQ AAVRELCEET GLADLDLLYL
     DVYEKDQVAH YVFTAQVPAS SEPSPQNEIA ACKWLAPQKL GDLKASSATK TIVKSYANES
     EGVSGARSHV TG
//
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