POA1_ASPCL
ID POA1_ASPCL Reviewed; 199 AA.
AC A1CNH7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE EC=3.1.3.84;
GN Name=poa1; ORFNames=ACLA_019030;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-beta-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 -!- SIMILARITY: Belongs to the POA1 family. {ECO:0000305}.
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DR EMBL; DS027059; EAW07198.1; -; Genomic_DNA.
DR RefSeq; XP_001268624.1; XM_001268623.1.
DR AlphaFoldDB; A1CNH7; -.
DR SMR; A1CNH7; -.
DR STRING; 5057.CADACLAP00002868; -.
DR EnsemblFungi; EAW07198; EAW07198; ACLA_019030.
DR GeneID; 4701859; -.
DR KEGG; act:ACLA_019030; -.
DR VEuPathDB; FungiDB:ACLA_019030; -.
DR eggNOG; ENOG502S60W; Eukaryota.
DR HOGENOM; CLU_054419_1_0_1; -.
DR OMA; NCQGSWG; -.
DR OrthoDB; 1416296at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..199
FT /note="ADP-ribose 1''-phosphate phosphatase"
FT /id="PRO_0000324901"
FT DOMAIN 1..199
FT /note="Macro"
FT BINDING 15..17
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 29..31
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 36..41
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168..174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 199 AA; 21718 MW; BBE10BC95867E93C CRC64;
MAHSPIHGRI TETEGDLFDA PDGAALIHAC NCQGSWGKGI AQAFKNKYPA AFTIYRAHCQ
NLLSKASYRT VNPVPDEGSL TGNSRKVRLP EGTALVIPPQ EHDHMGRHKK HWIICLFTSR
GFGRGVSSPA VIIQNTELAV VDMRRQIAEL HAEEGLGGFS GELWSCRFNS GLFGVDWALS
RKVLEDAGLE VTVVSPREG
