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Database: UniProt
Entry: A0A0Q5VK87_9CAUL
LinkDB: A0A0Q5VK87_9CAUL
Original site: A0A0Q5VK87_9CAUL 
ID   A0A0Q5VK87_9CAUL        Unreviewed;       136 AA.
AC   A0A0Q5VK87;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Phosphohydrolase {ECO:0000313|EMBL:KQS56632.1};
GN   ORFNames=ASG17_10180 {ECO:0000313|EMBL:KQS56632.1};
OS   Brevundimonas sp. Leaf363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS56632.1, ECO:0000313|Proteomes:UP000051182};
RN   [1] {ECO:0000313|EMBL:KQS56632.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS56632.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS56632.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS56632.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQS56632.1}.
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DR   EMBL; LMPZ01000002; KQS56632.1; -; Genomic_DNA.
DR   RefSeq; WP_056103424.1; NZ_LMPZ01000002.1.
DR   AlphaFoldDB; A0A0Q5VK87; -.
DR   STRING; 1736353.ASG17_10180; -.
DR   OrthoDB; 9761969at2; -.
DR   Proteomes; UP000051182; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd04673; Nudix_Hydrolase_15; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051182}.
FT   DOMAIN          2..130
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   136 AA;  14920 MW;  25F5144BF9611EC6 CRC64;
     MTPTPVVGVV CFRDGEVLLI RRANPPRQGE WSLPGGRIEP GEPVLDAAHR ELREETGVEA
     ALIGLIDVVD GVFPEHERHY VLIDYAMRWT AGEPVAGDDA SEARFFPIDA AAMLVEWSET
     ERIIRTGAAL NRSVSS
//
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