ID N1Q7U9_PSEFD Unreviewed; 833 AA.
AC N1Q7U9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EME88840.1};
GN ORFNames=MYCFIDRAFT_149398 {ECO:0000313|EMBL:EME88840.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME88840.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME88840.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME88840.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB446555; EME88840.1; -; Genomic_DNA.
DR RefSeq; XP_007921718.1; XM_007923527.1.
DR AlphaFoldDB; N1Q7U9; -.
DR STRING; 383855.N1Q7U9; -.
DR GeneID; 19331451; -.
DR KEGG; pfj:MYCFIDRAFT_149398; -.
DR eggNOG; KOG0789; Eukaryota.
DR HOGENOM; CLU_001645_11_0_1; -.
DR OrthoDB; 1342035at2759; -.
DR Proteomes; UP000016932; 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:UP000016932}.
FT DOMAIN 236..352
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 487..820
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 679..811
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 93056 MW; 6C50D44B83C27906 CRC64;
MTSPQRRQPP HTPSPNYFAF HTDASSFLTD TPHHAKNNWS PPSSTVRSTA AISPSVVPLD
QSPEYEAFRK QSESSKTFSL GGLNNFKMTM PASSTPSSRP SRDRTSSRSS VHKSSKSGTT
PRDIPIASHR NMLDTSHGLS HSPKRVLSPG SKTESRRRGS PPTFDGVTGQ AQTESPQTES
PKSAGSEHHR FQLPLDNLTA SYNATKTRAD TIPLTSDGDD RFMVPPQHVI NLINSKGDNI
LLLDLRVQTQ YAHSRIMTAL NLCIPTTLLK RPSFNVHKLA DTFNDEIQRA RFENWRKSSH
IIVYDGNSSA LKDATICMNT IKKFQGEGFG GTLFIIRGGF NEFAKTFPAY IESGADASPG
GAANGVDNDG PKVAPVIGGC PMPSTDKPAN PFFGNIRQNM DLIGGVGQIP IKHPNKETKS
AEEEYPHWLK SVAEERNQGQ TVSQRFEQIE RREKKRMEDA LSGNVSWGTP KQETGGSVRI
AGLEKGNKNR YNNIWPFEHS RVKLQGVPSH GCDYFNASHI KAAWSNKRYI STQAPIPATF
NDFWDVVWQQ DVRVIVMLTA EKEGAQVKAH NYWDEKQYGS IHLEFLSEKR ASLEPSRIKR
HQKRPWAVKR HSTNSSNPQV PLATIDGKEE KGGDQPYVIV RKFLVRHDRF AFEPPREVTQ
LQYSNWPDFG APAHPAHLLG LVEQTNAVVR ANNKTNSSEP EPPNKRPVLV HCSAGCGRTG
TFCTVDSVID MLKRQHISRN SRQGTPMDID KQPPRKESGG GFFASQSQYQ ENSEAIDGPW
TQKDDLDLVE KTVEDFRHQR ISMVQSLRQY VLCYESIMEW LVQERESAKA ATD
//
