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Database: UniProt
Entry: A0A094G6T7_9PEZI
LinkDB: A0A094G6T7_9PEZI
Original site: A0A094G6T7_9PEZI 
ID   A0A094G6T7_9PEZI        Unreviewed;       880 AA.
AC   A0A094G6T7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Rhodanese domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V497_00336 {ECO:0000313|EMBL:KFY67557.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY67557.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY67557.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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:KFY67557.1}.
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DR   EMBL; JPJZ01000043; KFY67557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094G6T7; -.
DR   STRING; 1420910.A0A094G6T7; -.
DR   HOGENOM; CLU_001645_11_0_1; -.
DR   OrthoDB; 1342035at2759; -.
DR   Proteomes; UP000029268; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029268}.
FT   DOMAIN          279..395
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          532..855
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          733..846
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   880 AA;  97570 MW;  8B270867D83E010C CRC64;
     MKAAARPPLR STRSHSHRQK TPSPAGGPLA QTIRAPSSAA PTISASFSPK RTPGGKEQAR
     PSSPNYFGIV VDAGSNGRDS GTGAKDNRSP TASSVQSYIE QTPRNIPLET SSDFDAFRKQ
     SEANHSFSLG HGNLSHFSSA PVLPAHAHGH KSTAGHDRNA EVKRTNSAVI VNSDAWLPPR
     SHSHTFPIEA SPIFGLPMQE SPMDTELSQP LAPVQEDMRS QHGDRHPRLS LPGDRPTPST
     PQRSQQDVIP RAETLPPVLH DGPAFISASD LRDFLSTQSS SEYLLLDLRV APQYSQSRIR
     NALNLCIPTT LLKRPSFNLA KLTDTFKDPE EKARFSKWNE CRYIVVYDAH SSDKKDAVSA
     MNTIKKFTNE GWNGRTYILK GGFKAFSAIQ SDAIDQNPTH DTQSSKNLSL GPLFPKATDV
     AGGCEMPQTK SVANPFFSNI RQNMDLVGGV GQIDVRRPDD VDHLADDFVP PWLQGATDRE
     DHGKTVSDKF LHIEQTELSR MQNALSSRVS YGTPTTRSEN DVQIAGFEKG GKNRYNNIWP
     FEHSRVRLQG RAEGACDYVN ATHIKPLWSN KRYIASQGPL PATFEDFWSV IWDQEVRVIV
     MLTAESEGGQ VKCHPYWSAQ EYGRFRISSS SEKKVPLEPI KHSHTSIRKE SFGRRRANTT
     IESSLPEASP GDNPDVVVRT ITLSCSTQPH APARQIMQLQ YSSWPDFGTT ARPSHLLGII
     ELANSLQHGS LPPAIASQIN SDEPEPDQSL PPMLVHCSAG CGRTGTFCTV DSVIDILKRQ
     RRESLNGVTP MDISTDEEAD YLSSKHQSKD MESDWLFNPN IDLIERTVAD LRKQRISMVQ
     SLRQYVLCYE TVLEWIFQQY QSPKRERSGS ESLASDERRG
//
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