ID A1DGR1_NEOFI Unreviewed; 130 AA.
AC A1DGR1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN ORFNames=NFIA_085210 {ECO:0000313|EMBL:EAW18568.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW18568.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
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).
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DR EMBL; DS027696; EAW18568.1; -; Genomic_DNA.
DR RefSeq; XP_001260465.1; XM_001260464.1.
DR AlphaFoldDB; A1DGR1; -.
DR STRING; 331117.A1DGR1; -.
DR EnsemblFungi; EAW18568; EAW18568; NFIA_085210.
DR GeneID; 4587023; -.
DR KEGG; nfi:NFIA_085210; -.
DR VEuPathDB; FungiDB:NFIA_085210; -.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_107716_1_0_1; -.
DR OMA; PVCRCTN; -.
DR OrthoDB; 21092at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:EnsemblFungi.
DR GO; GO:0016311; P:dephosphorylation; IEA:EnsemblFungi.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR10828:SF38; ARSENICAL-RESISTANCE PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT DOMAIN 15..117
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 130 AA; 14991 MW; 155AFA4ECE427AA1 CRC64;
MTRDALSELL LSTSSPNKLA IIDVRDQDHI GGHIYSSTWV PSSSLDYRMP ELVRTLKDKE
KVVFHCALSQ QRGPSAALRY VREREAALGP EKSKKQQVYV LEGGFVQWQE KYGKDTRLTE
AYVEDIWREY
//
