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Database: UniProt
Entry: I2K221_DEKBR
LinkDB: I2K221_DEKBR
Original site: I2K221_DEKBR 
ID   I2K221_DEKBR            Unreviewed;       507 AA.
AC   I2K221;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 2.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   ORFNames=AWRI1499_0764 {ECO:0000313|EMBL:EIF49273.1};
OS   Brettanomyces bruxellensis AWRI1499.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Brettanomyces.
OX   NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF49273.1, ECO:0000313|Proteomes:UP000004997};
RN   [1] {ECO:0000313|EMBL:EIF49273.1, ECO:0000313|Proteomes:UP000004997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF49273.1,
RC   ECO:0000313|Proteomes:UP000004997};
RX   PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA   Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT   "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT   Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL   PLoS ONE 7:E33840-E33840(2012).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class CDC14 subfamily. {ECO:0000256|ARBA:ARBA00007315}.
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:EIF49273.1}.
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DR   EMBL; AHIQ01000059; EIF49273.1; -; Genomic_DNA.
DR   Proteomes; UP000004997; 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:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14499; CDC14_C; 1.
DR   CDD; cd17657; CDC14_N; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR044506; CDC14_C.
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:UP000004997}.
FT   DOMAIN          176..334
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          255..320
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          363..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   UNSURE          96
FT                   /note="I or L"
FT                   /evidence="ECO:0000313|EMBL:EIF49273.1"
FT   UNSURE          363
FT                   /note="E or Q"
FT                   /evidence="ECO:0000313|EMBL:EIF49273.1"
FT   UNSURE          375
FT                   /note="D or N"
FT                   /evidence="ECO:0000313|EMBL:EIF49273.1"
FT   UNSURE          413
FT                   /note="D or N"
FT                   /evidence="ECO:0000313|EMBL:EIF49273.1"
FT   UNSURE          502
FT                   /note="I or L"
FT                   /evidence="ECO:0000313|EMBL:EIF49273.1"
SQ   SEQUENCE   507 AA;  57696 MW;  705C9FC23EDD7570 CRC64;
     MHHKLXTDAI EFLKNKVYLG SYDQAPENSS SFVYFTVEDA LPYNAFHLDF GPLHIGHLYR
     FAVXLHNILN DPXNSSKAVV FYSSSSAKAR ANAACLLCCY LVLVQDWAPH QVLQPISQIQ
     PPLMPFRDAG YSKADFELSI QDVVYGIWRA KERNMIDITN FNLEEYEQYE RVDQGDFNLI
     CDEFIAFASP RQSRPGAPLN QPFRKLLXYF VSHNVELVVR LNTHLYDKNE FEKRGIKHLD
     MIFEDGTCPT MELVQKFIGA SETIISNGGK IAVHCKAGLG RTGCLIGAYL IYTHGFTANE
     CIGYMRMMRP GMVVGPQQHW LYLHQNEFRD WRHTMVLDTX PDKSIGXLFP LIPLDAYKER
     RRERRXMEXE RXNMDMNDAD IPADESVXIS SMGGRRKVST QLRQAASEAI PSDNPGQPRK
     YIGRNGRYTN SDEERDNEDD APYTSTVGNN AISSSPRKXM XXFNENQENV VPXVDGDSDV
     FMGDKDXKVS THSTRKTXNS LLTYKAS
//
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