ID A0A0S9CMR5_9MICC Unreviewed; 324 AA.
AC A0A0S9CMR5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=NUDIX hydrolase {ECO:0000313|EMBL:KQN94948.1};
GN ORFNames=ASE96_01790 {ECO:0000313|EMBL:KQN94948.1};
OS Arthrobacter sp. Leaf69.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN94948.1, ECO:0000313|Proteomes:UP000051467};
RN [1] {ECO:0000313|EMBL:KQN94948.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN94948.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN94948.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN94948.1,
RC ECO:0000313|Proteomes:UP000051467};
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:KQN94948.1}.
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DR EMBL; LMLR01000001; KQN94948.1; -; Genomic_DNA.
DR RefSeq; WP_056425133.1; NZ_LMLR01000001.1.
DR AlphaFoldDB; A0A0S9CMR5; -.
DR STRING; 1736232.ASE96_01790; -.
DR OrthoDB; 4287477at2; -.
DR Proteomes; UP000051467; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03673; Ap6A_hydrolase; 1.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
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; PTHR21340; DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT; 1.
DR PANTHER; PTHR21340:SF8; NUDIX HYDROLASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 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 18..146
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 324 AA; 35284 MW; CF8870536704BDDF CRC64;
MSSDALVADQ TDHPGEEIAV VAAGAVPWRV TAGGKDLEVL LIHRPRYDDW SWPKGKIDPG
ETVPECAARE VDEEIGLKAP LGIPLPPIHY HVPAGLKVVH YWAVDVDGAA LLPDGKEVDS
VMWCSPEKAA RLLSNPSDVG PLEHLAAAHA RGELKTWPLL VVRHAKAKPR SSWSKAEGDR
PLAATGLRQA QAVGRLLQAW KPMRVVSSPW LRCVATIAPY AKATDAKVKL NEALTEHRHG
RHPHKTAAAV EGLFDKQRAV ALCTHRPALP TVFAQLAKHM GSRLRGQLPD SDPFLAPGEI
VVCHVAHHSK DKVVAVERFR PFDD
//
