ID   Q1YU47_9GAMM            Unreviewed;       241 AA.
AC   Q1YU47;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=NUDIX hydrolase {ECO:0000313|EMBL:EAS48211.1};
GN   ORFNames=GB2207_10381 {ECO:0000313|EMBL:EAS48211.1};
OS   gamma proteobacterium HTCC2207.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Porticoccaceae; SAR92 clade.
OX   NCBI_TaxID=314287 {ECO:0000313|EMBL:EAS48211.1, ECO:0000313|Proteomes:UP000005555};
RN   [1] {ECO:0000313|EMBL:EAS48211.1, ECO:0000313|Proteomes:UP000005555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2207 {ECO:0000313|EMBL:EAS48211.1,
RC   ECO:0000313|Proteomes:UP000005555};
RA   Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:EAS48211.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAPI01000001; EAS48211.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1YU47; -.
DR   STRING; 314287.GB2207_10381; -.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_059078_2_1_6; -.
DR   OrthoDB; 9788263at2; -.
DR   Proteomes; UP000005555; Unassembled WGS sequence.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02883; Nudix_Hydrolase; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 2.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR039121; NUDT19.
DR   PANTHER; PTHR12318:SF0; ACYL-COENZYME A DIPHOSPHATASE NUDT19; 1.
DR   PANTHER; PTHR12318; TESTOSTERONE-REGULATED PROTEIN RP2; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EAS48211.1}.
FT   DOMAIN          8..155
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   241 AA;  26110 MW;  63C1A04A74313FE7 CRC64;
     MSDTAADILR NAATVMILRQ AQTGIEILLL RRNAKLAFAG GAWVFPGGAV DAADCAGAGI
     EDESLTARVA AVRESAEECG LVLEAEHLVH FSHWTTPEKL TRRFATWFFA AVVSEADSTV
     VIDDGEIHDF QWLNPSQALA MHDAGELDMM PPTYMSIKLV DQFVSAEEAL ESLRQFDAYW
     VTPRFARDGE VGVLLYPGDA GYETQNGSLA GPRHRCILGN KGVSYIHSGA DVGIAVMDNP
     Q
//