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Database: UniProt
Entry: B3LRJ2_YEAS1
LinkDB: B3LRJ2_YEAS1
Original site: B3LRJ2_YEAS1 
ID   B3LRJ2_YEAS1            Unreviewed;       928 AA.
AC   B3LRJ2;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Tyrosine phosphatase {ECO:0000313|EMBL:EDV08905.1};
GN   ORFNames=SCRG_04551 {ECO:0000313|EMBL:EDV08905.1};
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV08905.1, ECO:0000313|Proteomes:UP000008335};
RN   [1] {ECO:0000313|Proteomes:UP000008335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR   EMBL; CH408052; EDV08905.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LRJ2; -.
DR   SMR; B3LRJ2; -.
DR   HOGENOM; CLU_007989_1_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd01446; DSP_MapKP; 1.
DR   CDD; cd18533; PTP_fungal; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF551; TYROSINE-PROTEIN PHOSPHATASE 3; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
FT   DOMAIN          111..232
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          530..878
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          798..869
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          247..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   928 AA;  105224 MW;  9BB710EDAF7E3940 CRC64;
     MKDSVDCPSI LPTDRTSVLS ETSTLVGSSS HVYSRHAPMN SYHNSMNSNI YHSPKASSPL
     VSYKTSSPVL LKRATAPVLP SFKPKEQRYN KPQGCSLITA VELGKIIETL PDEKVLLLDV
     RPFTEHAKSI ITNSIHVCLP STLLRRKNFT FSKLLDNLTP SEQSVLKSKL AIDNLRIIIY
     DSTANQTESS VSLPCYGIAS KLIEFDTNVK KTVSILMCGF PQFKILFPDH INTNTFNSDC
     ISSAEPKSPK TNLMNSLHNT APHMTATTPL SSPQMNLKLK VPDDSRSDHS NFSSSPSPRN
     VLSDSPMSSS SPISALFKFQ LPAPQTNINQ MFKFSQNEEI MGLETYLSAV NIKEEHERWY
     NNDSAKKSLQ NFQFPKNQNS LEKDTNKDKL GFQIRYENLS KNYEKEVIDS VIPEWFQHLM
     SIPKIELVSQ FQKLDFLEKR RLNHSVSFRK KENSFILEKP SSYPEQLTST SSSTIMPPKF
     PDVNKVQKRS HSQPIFTQYS KYKSMLSLES DSDSESDDVI ISSGVELGAK NRYKDIFPYE
     HSRVILKKGL QSSKGIKHSH STSDGGILDN YINANYLSLP RFSVEQNSSF QTTTTTTRRV
     RYIATQAPMP STVHDFYTCI LNNGVPLVLS LTNDFENGIE KCYRYWQEGN YNGIHVKLLE
     KKILKMPSTT SMRKNTMGTQ NSSLYSAGVQ GNSSNYSTDN DNDNDNNNNN NNNSNIAVTA
     AACDDDDDDD DDAILIRKIL LTYHDQEKPY ELLQIQVKNW PDLGTLLNPI SILQAINVKN
     HIIDTLFARN YYQNDQLPTI LVHCSAGCGR TGTLCTIDSI LSNFEMFEML QKEFVKLKYP
     AKLFDPISWT INIFRKQRIS MVQNINQFIF IYDCLLFYFR LRLDDITERT DGDGSNKDNI
     SLSALIEQIE KLEILQTFVD DKLKELPQ
//
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