ID A0A1R3RL89_ASPC5 Unreviewed; 627 AA.
AC A0A1R3RL89;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=ADP-ribose 1''-phosphate phosphatase {ECO:0000256|ARBA:ARBA00019744};
DE EC=3.1.3.84 {ECO:0000256|ARBA:ARBA00012983};
GN ORFNames=ASPCADRAFT_49272 {ECO:0000313|EMBL:OOF95254.1};
OS Aspergillus carbonarius (strain ITEM 5010).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=602072 {ECO:0000313|EMBL:OOF95254.1, ECO:0000313|Proteomes:UP000188318};
RN [1] {ECO:0000313|Proteomes:UP000188318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 5010 {ECO:0000313|Proteomes:UP000188318};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV907500; OOF95254.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3RL89; -.
DR VEuPathDB; FungiDB:ASPCADRAFT_49272; -.
DR OMA; IHACNCR; -.
DR OrthoDB; 2718868at2759; -.
DR Proteomes; UP000188318; 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; IPR040459; MJ1316.
DR InterPro; IPR014347; Tautomerase/MIF_sf.
DR PANTHER; PTHR12521:SF0; ADP-RIBOSE GLYCOHYDROLASE OARD1; 1.
DR PANTHER; PTHR12521; PROTEIN C6ORF130; 1.
DR Pfam; PF04457; MJ1316; 1.
DR SMART; SM00506; A1pp; 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:UP000188318}.
FT DOMAIN 437..627
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 169..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 69625 MW; EBF939B76D90F179 CRC64;
MASDLPSETQ QGLHNVPEQS TERTPTPQPE ARTRSPTPTP ESDYTPFRSA RSKPEPVENR
LRPAADIINR IIWDEAFDPA NYIIGYEDRF EGRLEAGFNS FTYAAMTSRR HRIDFSLRRR
RNDPSLTSSG SVSPTVPVLQ SPVTFQAFAS VNFSEATLKQ KNKLERAPVR PSMFLEEKDD
DETPTPALAG GAPVDLKSSH VDRKSAEEKP MTRTKSQYFE DAFSTRGPLI SPRSQISQDS
VVVVEIKINT KKSETLMMTT IQEEACIHFG RSSLPAYLMK VFALPYLIAP ITNLRSTILI
QAALQEIIHV APSRGVILYI PISEENFATN GVTMMGELAR LERTSPDHGP GLFRSISRTM
SRRMKSSSSQ SAPISVTTTS SWACGGGGTQ ASSVTGKESQ CSDALRDEGK PNSGTKPKGF
RHFLSRQGSE RLQHPSNNQQ MESSTVHGRV SEIQGNIFDA PDGAGLIHAC NCRGSWGKGI
AKAFRERYPT AYEIYRSHCR RCSSGPRYNP VLIDGGARQI RVPEGTALII PPQKKDHEAG
ISKRHWIICL FTSRGFGRMV SPEETILENT ELAVADMQRQ LDQLEDGVSE LWSCQFNSGL
FGVEWARSKE IVERSGLKFT VVRPKKE
//
