ID A0A1B8EGZ3_9PEZI Unreviewed; 224 AA.
AC A0A1B8EGZ3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00012983};
DE EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN ORFNames=VF21_10284 {ECO:0000313|EMBL:OBT70623.1};
OS Pseudogymnoascus sp. 05NY08.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT70623.1, ECO:0000313|Proteomes:UP000092096};
RN [1] {ECO:0000313|EMBL:OBT70623.1, ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|EMBL:OBT70623.1,
RC ECO:0000313|Proteomes:UP000092096};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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; KV459105; OBT70623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8EGZ3; -.
DR STRING; 1622149.A0A1B8EGZ3; -.
DR OrthoDB; 1105329at2759; -.
DR Proteomes; UP000092096; Unassembled WGS sequence.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
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 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:UP000092096}.
FT DOMAIN 1..122
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 124..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 224 AA; 23870 MW; C353D8CB79EBC291 CRC64;
MRGCKTGSAK ITGAYELPCK KVIHAVGPVY SRSDREKSAE LLASCYTTSL QLAVDNDCKS
VVFSGLSTGV YGYPSQDAAS VATKAVRGFL EGASGDKIDR VIFCTFEMKD VNAYNDWVPR
AFPPAEQDLK EGGEANESNQ AEDSDKAEKA EKDEQAEKTE KDEKAEKDER AGVVGAGETA
VGDASGNLSK SHTTVDDLPE VPKAEPSAGD GPEPKRQKQQ PSDS
//
