ID A0A165HKS6_XYLHT Unreviewed; 630 AA.
AC A0A165HKS6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=L228DRAFT_238197 {ECO:0000313|EMBL:KZF23662.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF23662.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF23662.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF23662.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000256|ARBA:ARBA00007315}.
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DR EMBL; KV407457; KZF23662.1; -; Genomic_DNA.
DR RefSeq; XP_018189217.1; XM_018331015.1.
DR AlphaFoldDB; A0A165HKS6; -.
DR STRING; 1328760.A0A165HKS6; -.
DR GeneID; 28896152; -.
DR InParanoid; A0A165HKS6; -.
DR OMA; KFERVDM; -.
DR OrthoDB; 9871at2759; -.
DR Proteomes; UP000076632; Unassembled WGS sequence.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF27; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632}.
FT DOMAIN 240..403
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 323..389
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 39..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 69637 MW; 8B0833A15C3BA972 CRC64;
MPSSPRGPSR LGMLPSFMTN CGQVLEYIQD RLYLASYENP PDENTPFPYP KEKKSPGKRS
KQTPVATPPP AGSAKGHAPV YFTVDYTLYY NSFHADFGPL HIGHLYRFAV QLHDILGDPA
NSERPVVLWS SPDSRNRANA ACILACYMVL IQNWPPHLAL APIAQMDPPP MPFRDAGYSQ
ADYTLSIQDV VYGVWKAKEE GLCGLMEFSL EEYEKFERVD MGDFNWLTPS FLAFASPQHS
PTAPIPPSSP LYAKLPTSVS AVMASDLPVS FKNVLSHFAT RDIGLVVRLN SELYSPSYFT
ALGINHLDMI FDDGTCPPLP LVKKFIKLAH EMINVKHKGI AVHCKAGLGR TGCLIGAYLI
YRHGFTANEV IAFMRFMRPG MVVGPQQHWL HLNQGTFREW WWEDSYKEKL AAMLPSTPTK
SSQKQRMRSQ GPTATPVNSK RAALGEIDSN ESSVATQDEN LPAPTPGQPR KGSRSHEPRH
HPYSRKISGV YDSDANVQQS AEFVSMHRQS RSDSESEEEW QLRMHSRRTA SRSPQSSDKK
RSVSYTTTTT TKASYSIGQA GESDIENYDG RPKTPTNSKS GSGSGAIGVA KVRSSPRRSA
DSRAAREAGV RKTSGRVGSM NGTLKSSGSK
//
