ID   A0A1V8UWB4_9PEZI        Unreviewed;       251 AA.
AC   A0A1V8UWB4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00019744};
DE            EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN   ORFNames=B0A51_04820 {ECO:0000313|EMBL:OQO27851.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO27851.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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:OQO27851.1}.
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DR   EMBL; NAEU01000145; OQO27851.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8UWB4; -.
DR   Proteomes; UP000192386; 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   SMART; SM00506; A1pp; 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:UP000192386}.
FT   DOMAIN          65..251
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..48
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  27184 MW;  002211A4F8B8E175 CRC64;
     MAVATRRIKA DSTSAITKET DTSSSIKKPT KKRPRSTQRP RRATRKSRTN TKATASMEAT
     STTQPTEDVP VKSTNLTIKE ETRDLFNSPP NSILLHACNC RGSWGAGVAA SFKKKYPAGY
     EVHVAHCKAT KAESLLGTAQ LIPPQASDAK SGESHWIACL FTSVDVGKKK GSRESILEAT
     GEAMQGLLKQ IGEVEDGVTI GSIRMPKINQ GLFDVPWERT RAVLEGIEVP ALLRKAGVEI
     VAVELEEEAK Q
//