ID A0A395HEP3_9EURO Unreviewed; 586 AA.
AC A0A395HEP3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00019744};
DE EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN ORFNames=BO80DRAFT_490510 {ECO:0000313|EMBL:RAL05468.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL05468.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL05468.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL05468.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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}.
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DR EMBL; KZ824421; RAL05468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HEP3; -.
DR VEuPathDB; FungiDB:BO80DRAFT_490510; -.
DR OrthoDB; 2718868at2759; -.
DR Proteomes; UP000249402; 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 Gene3D; 3.30.429.10; Macrophage Migration Inhibitory Factor; 1.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR014347; Tautomerase/MIF_sf.
DR PANTHER; PTHR12521:SF0; ADP-RIBOSE GLYCOHYDROLASE OARD1; 1.
DR PANTHER; PTHR12521; PROTEIN C6ORF130; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF55331; Tautomerase/MIF; 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:UP000249402}.
FT DOMAIN 393..586
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 65092 MW; 65A17E0B09B2F78E CRC64;
MASDLPSETQ QGLHDVPEQD RERTPTPQPE AQSRTPTPTP ETDYTPFKST ISKPEPVENR
LRPAADIINR IIWDPAFDPA NYIIGRHRID FSLRRRRNNP SLTSSGSLSP TVPVLQSPVT
FQAFATVNVS ETTIKQKNKL ERTPVKPSMF LEEKDDDDTP VPALAGRAPV DVKSAQVERK
SVEERPTTRT KSQYFEDAFS TRGPLSSPRS QISQDSVVVV EIKMNTKTLM MTTIQEDACI
HFGRSSLPAY LMKVFALPYL IAPITNLRST ILIQAALQEI IHVAPNRGVI LYIPISEENF
ATNGVTMMGE LARLERSSTD HGPGLFKNIS RTMSRRLKSS SSQSAPISVA TTSSWACGNG
TQASSMTGKE SQCSDTLKDE GKPKTSRKPV HSDIVPMESS STHGRVAEIQ GNIFDAPDGA
GLIHACNCRG SWGKGIAKAF RQRYPAAYEI YRSHCRKCSF SLRYNNVPNE GGTRKVRVPE
GTALIIPPQK KDYEGGMSKR HWIICLFTSR GFGRKVSPEE IVLKNTELAV ADMQRQLDQL
REGEGDVSEL WSCRFNSGLF GVEWARSRDI LEKTGLEITV VRPNEE
//
