ID Q6BSM6_DEBHA Unreviewed; 641 AA.
AC Q6BSM6;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=DEHA2D07678p {ECO:0000313|EMBL:CAG86938.1};
GN OrderedLocusNames=DEHA2D07678g {ECO:0000313|EMBL:CAG86938.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG86938.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG86938.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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DR EMBL; CR382136; CAG86938.1; -; Genomic_DNA.
DR RefSeq; XP_458794.1; XM_458794.1.
DR AlphaFoldDB; Q6BSM6; -.
DR STRING; 284592.Q6BSM6; -.
DR GeneID; 2901224; -.
DR KEGG; dha:DEHA2D07678g; -.
DR VEuPathDB; FungiDB:DEHA2D07678g; -.
DR eggNOG; KOG4667; Eukaryota.
DR HOGENOM; CLU_444876_0_0_1; -.
DR InParanoid; Q6BSM6; -.
DR OMA; DFRGCGN; -.
DR OrthoDB; 159937at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR029058; AB_hydrolase.
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:SF1; PTP_DSP-LIKE; 1.
DR PANTHER; PTHR31126; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR Pfam; PF13350; Y_phosphatase3; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT DOMAIN 469..543
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 641 AA; 73000 MW; E2EF3AB989C7CE38 CRC64;
MTVSVPREIE VTLGKGVSGT LTVPHSADSE SPFEQNYAPT TNKAAIILHG QGGHRSYCYQ
KMLAHKLASD LGIYSLRIDF RGCGNSADNA DEKIARIIGQ DIEDIQASAE FLLDSKQNPL
GMRFMVSSII GHSRGGVAMF LWALEQDKIL KSPDPSKAIV VPNLVNCSAR YRSDTVYDRY
PHDFEGAYLR SLRYGEIQKV FVSKDEIDSL AAPDMSALRD LSTDFSVLSV YGLEDRIIPV
NDGSFYANVL NRGPYSHHLE LIPFADHNFY GIEPIETDDD AEDYNPHNLP LNSKKLANHN
VMVTSIIIDY LKPENELNRF LYRSFNVGYI PRWKQIDGIS NFRDIGAWKI QNPTYRLPNY
DNESHYYVKP HIAFRCANTA DVTQMGLKEL RKLNVKVMFD FRSSIEINND GSPQNLEKYG
IKRIHAPVFS ETDYSPEVIA IRYTNLMTSW FTYVNVYEDI LENGTSAFRQ VFEFIRDEVP
ASSFVFHCTA GKDRTGVLSM LILLFLGVDK HTISKEYELT TVGLKNDHAS IRDKFIKTME
NFKTKMENVE DVAQIIAQGR KGWTIEEDGF QNLISSRYEA MLATIELFNQ KYGSIVNYMK
TQLKFEDSDL LKIYENLVYV SEINKPEPNP MFNLVEFAPK L
//