ID Q6CU45_KLULA Unreviewed; 983 AA.
AC Q6CU45;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=KLLA0C07733p {ECO:0000313|EMBL:CAH01395.1};
GN ORFNames=KLLA0_C07733g {ECO:0000313|EMBL:CAH01395.1};
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590 {ECO:0000313|EMBL:CAH01395.1, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAH01395.1, ECO:0000313|Proteomes:UP000000598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC WM37 {ECO:0000313|Proteomes:UP000000598};
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).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR EMBL; CR382123; CAH01395.1; -; Genomic_DNA.
DR RefSeq; XP_452544.1; XM_452544.1.
DR AlphaFoldDB; Q6CU45; -.
DR STRING; 284590.Q6CU45; -.
DR PaxDb; 284590-Q6CU45; -.
DR GeneID; 2891831; -.
DR KEGG; kla:KLLA0_C07733g; -.
DR eggNOG; KOG0789; Eukaryota.
DR HOGENOM; CLU_007989_1_0_1; -.
DR InParanoid; Q6CU45; -.
DR OMA; KDWPDLG; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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; 1.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000000598}.
FT DOMAIN 182..309
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 587..938
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 810..929
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 983 AA; 110069 MW; 38BE93C93B4B903D CRC64;
MEYIDTMGTN KQQEEIQLKE PLSFSRPLAR PPSISGCTEY KDRDSIQSSS FTSESSSVLS
SSSTLIDDKS SNSSLASPAL SANYKRNSTE VLPEKILIHA STFPSASEPS YSTCTPSPLS
ASHRSSLSFS RSRSRSIAMK SNSLPAIPTI CPKDLRFPKH KDCSFISPAD LHHYIENMDQ
NPNEKLIIFD TRPFIEFNKN HIRSAMHLCL PSTLLKRKNF NLERLIGNLP SPGRETLSEY
LLGSDSATAN AKVVIYDNVA NQTDYAVSLA CFGISSKILD HVSDKQKPSV FILAEGFESF
NAAYPDDVEV GTMDLEDSYT LDSPSSPHQA DNISPVQPQL KHSGRSHSHS CSPLKQPPQT
GNSRTLSGSP ISTSSPLSSL FGFKLPAPIN NQHLPTFKLP QIEHDISDLD NYVKAVEINE
RSQRNSFLES ENDLRSFKFP ASPSKQFSTD ATSSSFTSTQ TALSPADPSS GHNSSKLNFQ
VKYDNLYHRF ASEEINQVVP SWFCQLMDIP KLHFISKFQR LELLERKRLQ RLLGPSSSAS
IVSTQSRSTV AGNDRCVEDG HYDVDEDDAE ENLQSITISS GVEFGTKNRY KDIFPYEHTR
VKLSHSSICS AGCENSTPSP RSSAYSSCAS GLPTQDEQED VWNTYINANY LVNPFAQLQQ
SSTADIKSVR YIATQAPLKE TISDFYTCIL NNNVPIILTL TDEFENGVEK CCNFWANGNY
DGINVKLLDE FSTMLQDKPM KAESNHEEDM FASKFWRHLK LNKTSDNNNE IIIRRIELSY
NNDRSKFQLL QLQIKDWPDL GTLLKPNEIL QIINLKNFVI DSLFAHNVYS PNYTPTVLVH
CSAGCGRTGT LCTVDSILSN LKKFDTDENP SLYGAFAVPL TPNLSPTTKS NSFSATKPPT
SLMFDPIVTT VNQFRRQRIS MVQNINQFLF IYDCLLFYFT LNLETSPTDP EKRNNWQSMT
DENSHLDILH KFIDGKVNEL QQV
//
