ID A0A0D1ZAN1_9EURO Unreviewed; 421 AA.
AC A0A0D1ZAN1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-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=PV11_05832 {ECO:0000313|EMBL:KIV83843.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV83843.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV83843.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV83843.1,
RC ECO:0000313|Proteomes:UP000053599};
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 Exophiala sideris CBS121828.";
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; KN846952; KIV83843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1ZAN1; -.
DR STRING; 1016849.A0A0D1ZAN1; -.
DR HOGENOM; CLU_046550_10_2_1; -.
DR OrthoDB; 1105329at2759; -.
DR Proteomes; UP000053599; 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:UP000053599}.
FT DOMAIN 38..218
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 283..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 46448 MW; AC014EB6BDA0A3FE CRC64;
MLLRLQTRAM SSGLRTAKDI PSISTLYRHK MLHPSRSEDL PTPNQQYNDK VCLIQYDITK
LEIDAIVNAA NRGLRGGGGV DGAIQRAAGP ELLKECATLG GCETGSAKIT DAYDLPCKKV
IHAVGPIFDS IEESEPLLRG CYRKSLSLAV ENGCRTIAFP NISCGVYGYP GRAAAHAACR
EVYAFLKKPE GQKLDKVIFC NFTGKDVEAY KEFLPILFPP TEDDLSHTGE FDHNEIVSPK
DNMPTVEQTH QKATYERLSP CPQGEILSQT WFRDMFSAYP DSDGYSSDDG WSVSSKRSMN
NEAQASPPPK KRKLGIQGLQ IREADDQEED CGPDGYDEAG NLGEIVDQTM NLKSVNQTTI
PESPGQLQDE TCFHSHFFKH DGFSTHGLWP HCAMICECHN KIIQARGTDM PSIGRGNPSQ
L
//
