ID A0A0S7DFF5_9EURO Unreviewed; 307 AA.
AC A0A0S7DFF5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Tyrosine specific protein phosphatases domain-containing protein {ECO:0000259|PROSITE:PS50056};
GN ORFNames=ALT_007238 {ECO:0000313|EMBL:GIM34974.1}, CNMCM8060_009228
GN {ECO:0000313|EMBL:KAF4181279.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM34974.1};
RN [1] {ECO:0000313|EMBL:GIM34974.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM34974.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4181279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4181279.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4181279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4181279.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GIM34974.1}.
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DR EMBL; BCLY01000001; GIM34974.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000008; KAF4181279.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DFF5; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_805; -.
DR OrthoDB; 933109at2759; -.
DR Proteomes; UP000713487; Unassembled WGS sequence.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR026893; Tyr/Ser_Pase_IphP-type.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR31126:SF10; PROTEIN PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G06650)-RELATED; 1.
DR PANTHER; PTHR31126; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR Pfam; PF13350; Y_phosphatase3; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 4: Predicted;
FT DOMAIN 180..251
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 87..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 307 AA; 34453 MW; D7D09355B8FA9899 CRC64;
MTSNLPRQSS VDLDSADRPF DNIINFRDVG RSINQLMGSR ILKEGVLFRS ARLDDASERD
RRRLAEELHI STVLDLRSMT EHQMATRKCR GEDALDPEQP SLPPSEANEH LMEIPGVQRS
LISLTGRAFE RALLWRLDWY NLIRVLALVA SGYRTEAVTI VGQQAMAPRG LIGLGQDTLD
SSTAEVREIF ELLVSPAAYP VIVHCTQGKD RTGLIVLLLL LLLPEVSAEA IAADYVKSEP
ELVVEFEERM KEIRVLGLDE EYTKCPPGFT QEIRAHLDAK YGGVEGYLMS VGIDREKQES
IRQRLLA
//