ID   A0A139II76_9PEZI        Unreviewed;       237 AA.
AC   A0A139II76;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   22-FEB-2023, entry version 19.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00019744};
DE            EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN   ORFNames=AC579_6701 {ECO:0000313|EMBL:KXT14256.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT14256.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT14256.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT14256.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) 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   -!- SIMILARITY: Belongs to the POA1 family.
CC       {ECO:0000256|ARBA:ARBA00006575}.
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:KXT14256.1}.
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DR   EMBL; LFZO01000088; KXT14256.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139II76; -.
DR   STRING; 113226.A0A139II76; -.
DR   Proteomes; UP000073492; Unassembled WGS sequence.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   CDD; cd02901; Macro_Poa1p-like; 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; PTHR12521:SF0; ADP-RIBOSE GLYCOHYDROLASE OARD1; 1.
DR   PANTHER; PTHR12521; PROTEIN C6ORF130; 1.
DR   Pfam; PF01661; Macro; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492}.
FT   DOMAIN          68..237
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   237 AA;  26034 MW;  4EBEAAC5AFADD4FB CRC64;
     MSSRGLRSAR KRKHEDMNGL DAAVDSSISQ PPKRSKTSNT TSKPQGRSKT RTDQTRSNPN
     KKSPNIQDKN MASSTGRTLT LTESTGDIFS AATPNTLLIH ACNTEGSWGA GIAAAFKSHY
     PSAYENYRDH CHMNGGELWR KAFLIPPARQ GECFVGCLFT SRSKGRKKDS PAQILGATGP
     AMRDLMRQVS ETETKIDEVR MCKINSGLFG VKWEKTKAVL EGIQGDFHDV KVISRGE
//