ID A0A1V2Q1M1_9PSEU Unreviewed; 172 AA.
AC A0A1V2Q1M1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=NUDIX hydrolase {ECO:0000313|EMBL:ONI82157.1};
GN ORFNames=ALI22I_39115 {ECO:0000313|EMBL:ONI82157.1};
OS Saccharothrix sp. ALI-22-I.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI82157.1, ECO:0000313|Proteomes:UP000188617};
RN [1] {ECO:0000313|EMBL:ONI82157.1, ECO:0000313|Proteomes:UP000188617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI82157.1,
RC ECO:0000313|Proteomes:UP000188617};
RX PubMed=28087533;
RA Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA Kuske C.R.;
RT "Polysaccharide degradation capability of Actinomycetales soil isolates
RT from a semi-arid grassland of the Colorado Plateau.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI82157.1}.
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DR EMBL; MTQP01000068; ONI82157.1; -; Genomic_DNA.
DR RefSeq; WP_077010625.1; NZ_MTQP01000068.1.
DR AlphaFoldDB; A0A1V2Q1M1; -.
DR STRING; 1933778.ALI22I_39115; -.
DR OrthoDB; 9816289at2; -.
DR Proteomes; UP000188617; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03673; Ap6A_hydrolase; 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; PTHR21340:SF0; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE [ASYMMETRICAL]; 1.
DR PANTHER; PTHR21340; DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT; 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:UP000188617}.
FT DOMAIN 1..158
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 172 AA; 19373 MW; 89FF634B9A37F908 CRC64;
MPQSSGRSGG PKPRRRNRRR GRRLKTVDET SAGGLVLDFE RHTAAIIGRL DRRGRLLWSL
PKGHIEAGET AEQTAVREVA EETGIHSRVL RPLGSIDYWF VAEDRRVHKT VHHFLLEALG
GELSDEDVEV TEVAWVPLGE LDERLAYADE RRLVRRAAEL LSEYQTDGAE SA
//