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Entry: C5MIC7_CANTT
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ID   C5MIC7_CANTT            Unreviewed;       802 AA.
AC   C5MIC7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EER30421.1};
GN   ORFNames=CTRG_05820 {ECO:0000313|EMBL:EER30421.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER30421.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER30421.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR   EMBL; GG692404; EER30421.1; -; Genomic_DNA.
DR   RefSeq; XP_002546342.1; XM_002546296.1.
DR   AlphaFoldDB; C5MIC7; -.
DR   STRING; 294747.C5MIC7; -.
DR   EnsemblFungi; CTRG_05820-t43_1; CTRG_05820-t43_1-p1; CTRG_05820.
DR   GeneID; 8300169; -.
DR   KEGG; ctp:CTRG_05820; -.
DR   VEuPathDB; FungiDB:CTRG_05820; -.
DR   eggNOG; KOG0789; Eukaryota.
DR   HOGENOM; CLU_007989_0_0_1; -.
DR   OrthoDB; 1342035at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
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   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:UP000002037}.
FT   DOMAIN          262..330
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          549..795
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          703..786
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   802 AA;  90954 MW;  B0F945576454C04B CRC64;
     MSKETMAFTF PNSNTSTQFK IPQPPITPTT NTTNNTNNFT SPLSQQQQQQ TPSTNTTPIR
     KRQPKHKSFN NSISSITSST SDLTIYESSI LSSKQLSTDT LIDEKQLPPL PPPPTSSASK
     HRYNQSLDSN RTLVSLDENE EDKFKFTINN NIDCNNNSNT SSSPIDSFFQ LSTPPPPIKD
     PQPDFFNQQH SRPKLPTMHS TPSLKKQVTL PSLSFDLSLK NIKQEQSKRL NYIPSQNFRP
     DIEKLSDRIQ YVCPIEFQGL CTAQDNLVID IRPFVEYSKS HVKSSLNICL PSTLLKRSNF
     SLIRSINSLP DFEKNRFTEF LNNTKGDLVV YDSTENSSNL YHICNKIITC ANFMTCPEKK
     ICLLDTNFSR FNELFPNAME TASPEVEDNN FLSPIIVPEK LRSSSVSDLS PYHKATPLSS
     SSSSSMLSAN TPILSANFTL PSKCKSFKIR HNEELPTIPC GNPFEENTAN LFKLSNIPSD
     CSKLPEWIKQ TIFDESGNPV TFKINNQFYS LEKLEQKRLI TALSLNTVND ISPMNEVAPK
     ISCGIEFGNK NRYKDIFLYD HSRVELGHVN NNPNDISNYI NASFIEPPEK YHHPESKYIA
     TQGPLDETMG DLWKLVLIRN IPLVISLTDS IENGIMKCAP FWQSGIYKSY EDTIRVTVVN
     NEEIDENLIV RTFKIKCNDE PSREVKQIQL LSWPDMGTTS DPRDILKVVG LKQKILAESS
     IKDKTTLVHC SAGCGRTGTL CVIDTLINYL KDNGDLNTEE EDPVFEITNH FRKLRISMVQ
     TLKQYYLIYE TLISYFDNKN QQ
//
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