ID Q0UQZ6_PHANO Unreviewed; 291 AA.
AC Q0UQZ6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00012983};
DE EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN ORFNames=SNOG_05818 {ECO:0000313|EMBL:EAT86882.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT86882.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: Highly specific phosphatase involved in the metabolism of
CC ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of
CC tRNA splicing. {ECO:0000256|ARBA:ARBA00002432}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-alpha-D-ribose 1''-phosphate + H2O = ADP-D-ribose +
CC phosphate; Xref=Rhea:RHEA:25029, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57967, ChEBI:CHEBI:58753; EC=3.1.3.84;
CC Evidence={ECO:0000256|ARBA:ARBA00034427};
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DR EMBL; CH445332; EAT86882.1; -; Genomic_DNA.
DR RefSeq; XP_001796215.1; XM_001796163.1.
DR AlphaFoldDB; Q0UQZ6; -.
DR STRING; 321614.Q0UQZ6; -.
DR EnsemblFungi; SNOT_05818; SNOT_05818; SNOG_05818.
DR GeneID; 5973092; -.
DR KEGG; pno:SNOG_05818; -.
DR VEuPathDB; FungiDB:JI435_058180; -.
DR eggNOG; KOG2633; Eukaryota.
DR HOGENOM; CLU_046550_3_1_1; -.
DR InParanoid; Q0UQZ6; -.
DR OMA; RTLDGCQ; -.
DR OrthoDB; 1105329at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0061463; F:O-acetyl-ADP-ribose deacetylase activity; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd02908; Macro_OAADPr_deacetylase; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR PANTHER; PTHR11106:SF120; ADP-RIBOSE GLYCOHYDROLASE MACROD1; 1.
DR PANTHER; PTHR11106; GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED; 1.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT DOMAIN 28..211
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 219..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 31970 MW; 4DF686F7B0BF9473 CRC64;
MAPVTLDDIP TLTKLYQDRT IVPDNDVSSS YTPSATLNDK ISIIRRDITT LAIDAIVNAA
NTSLLGGGGV DGAIHRAAGP KLYDECETLD GCETGNAKMT RGYELPSKKV IHAVGPIYWK
EGRSASAKLL SMCYRTSLQL AVDNECRSIA FSALSTGVYG YPSDEAAVVA LQTVRQFLDE
DGKAEKLDRV IFCNFLEKDE NAYYREIQKY FPMVQSVEDT AGQDEPDAPV ETSTEPSEIL
SQLPDAPTED PKDITDIEEP STKKQKTEDT DDDFVVVEKE DAKEDKPKPE L
//
