ID W2S2A0_9EURO Unreviewed; 350 AA.
AC W2S2A0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN ORFNames=HMPREF1541_01994 {ECO:0000313|EMBL:ETN42836.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN42836.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN42836.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN42836.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) 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};
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DR EMBL; KB822718; ETN42836.1; -; Genomic_DNA.
DR RefSeq; XP_008714572.1; XM_008716350.1.
DR AlphaFoldDB; W2S2A0; -.
DR STRING; 1220924.W2S2A0; -.
DR GeneID; 19969333; -.
DR VEuPathDB; FungiDB:HMPREF1541_01994; -.
DR eggNOG; KOG3904; Eukaryota.
DR HOGENOM; CLU_018689_0_0_1; -.
DR InParanoid; W2S2A0; -.
DR OrthoDB; 52409at2759; -.
DR Proteomes; UP000030752; 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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752}.
FT DOMAIN 23..232
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 38605 MW; 3A87C4F26958D880 CRC64;
MASSNPKPKF EVREYTTHKN PAPASPSASI ILVSPTNEIL LLHRVKSSSA FPSAHVFPGG
NLDPQDGELP SEPTDPARHK DSSAYRTGAI RELFEETGIL LAKESTSATS LLPVSPEARL
AGRKAVHSGK ISFKDWLSSQ SKDAVLHTEG LIPFTHWVTP PNVPKRFTTQ MYLYFVHLKE
TSNPSIHATA DQIETMAPEY RPAADWLRAA QAGDVILFPP QFILLYLASQ FLDRVDQLEG
SKEIYGAKTT AMDIVKRRRA LYEFVTKPGQ NGGPAWSEKF ISPIGKGVQH DGRQALALGK
PGPELKDSGL SGDEEYVVMV KFQKEGPRQL EVRRKSEVAE EGRKAKPEKL
//