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Database: UniProt
Entry: A0A0D2IKK5_9EURO
LinkDB: A0A0D2IKK5_9EURO
Original site: A0A0D2IKK5_9EURO 
ID   A0A0D2IKK5_9EURO        Unreviewed;       347 AA.
AC   A0A0D2IKK5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00012983};
DE            EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN   ORFNames=Z520_07014 {ECO:0000313|EMBL:KIX97561.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX97561.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX97561.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX97561.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-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};
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DR   EMBL; KN848074; KIX97561.1; -; Genomic_DNA.
DR   RefSeq; XP_016631684.1; XM_016777513.1.
DR   AlphaFoldDB; A0A0D2IKK5; -.
DR   STRING; 1442371.A0A0D2IKK5; -.
DR   GeneID; 27712760; -.
DR   VEuPathDB; FungiDB:Z520_07014; -.
DR   OrthoDB; 1105329at2759; -.
DR   Proteomes; UP000053411; 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; GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED; 1.
DR   PANTHER; PTHR11106:SF27; MACRO DOMAIN-CONTAINING PROTEIN; 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:UP000053411}.
FT   DOMAIN          35..215
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   REGION          222..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  37111 MW;  12EAA18E95F17B5B CRC64;
     MAFRPLSSKI PIPVEDIPTL SFLYNNDQLN PSVEEGLPSP NQDFNNKICV IQADITKLKV
     DAIVNAANRG LRGGSGVDGA IQRAAGPRLL QECATLGGCE TGSAKITEAY NLPSRKVIHA
     VGPVFEDHET SEPLLRGAYR TALNLAVEHG CKSIAFPAIS TGVYGYPSRD AARAAISEVR
     AFLGGPKGLQ IEKVVFCNFV QKDVDAYARF LPLSFPPTPD DLSHTGEYDF DTDDLNKENS
     PTDAQALLGA KSERAVNRSS RAIVQRHARR TFTNSDRAQL YFDGAGGDPA CPEGDDVAVD
     ENDGDVETRG GDDGQGPAEA GTSGKVSIKT TRGSTFWVTY AKRGHAV
//
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