ID   A0A1Q8RT49_9PEZI        Unreviewed;       249 AA.
AC   A0A1Q8RT49;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00012983};
DE            EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN   ORFNames=CCHL11_06179 {ECO:0000313|EMBL:OLN87500.1};
OS   Colletotrichum chlorophyti.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN87500.1, ECO:0000313|Proteomes:UP000186583};
RN   [1] {ECO:0000313|EMBL:OLN87500.1, ECO:0000313|Proteomes:UP000186583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTL11 {ECO:0000313|EMBL:OLN87500.1,
RC   ECO:0000313|Proteomes:UP000186583};
RA   Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT   "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT   herbaceous plants.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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};
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:OLN87500.1}.
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DR   EMBL; MPGH01000091; OLN87500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q8RT49; -.
DR   STRING; 708187.A0A1Q8RT49; -.
DR   OrthoDB; 1105329at2759; -.
DR   Proteomes; UP000186583; Unassembled WGS sequence.
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:UP000186583}.
FT   DOMAIN          26..208
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   REGION          217..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  26455 MW;  8BB08430B17A00C1 CRC64;
     MAITAVADIP TVELLYKLGK LSTPTKPLYS PNVSHNQKVA VFRGDITKLG VDAIVNAANS
     SLRGGGGVDG AIHRAAGPGL LQECKRLNGC STGSAKITDA YNLPCKKVIH AVGPVYDELS
     PEFSEEKLRG CYQTSLDLAV QNGCRSIAFS AISTGVYGYP SREAAPVAAD VVRTFLDGEK
     GKKLDKVVFC TFEMKDVNAY NETLPRFFPL DDISVSADET SESPSKQEAE EAKAIAAELP
     SVPKADPSQ
//