ID C5FDE1_ARTOC Unreviewed; 453 AA.
AC C5FDE1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Protein-tyrosine phosphatase 2 {ECO:0000313|EMBL:EEQ27915.1};
GN ORFNames=MCYG_00803 {ECO:0000313|EMBL:EEQ27915.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ27915.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR EMBL; DS995701; EEQ27915.1; -; Genomic_DNA.
DR RefSeq; XP_002850699.1; XM_002850653.1.
DR AlphaFoldDB; C5FDE1; -.
DR STRING; 554155.C5FDE1; -.
DR GeneID; 9226629; -.
DR VEuPathDB; FungiDB:MCYG_00803; -.
DR eggNOG; KOG0789; Eukaryota.
DR HOGENOM; CLU_001645_9_12_1; -.
DR OMA; HYLFAGW; -.
DR OrthoDB; 1342035at2759; -.
DR Proteomes; UP000002035; 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 InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
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:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 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; SSF48371; ARM repeat; 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:UP000002035}.
FT DOMAIN 54..356
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 265..347
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 50606 MW; 8542F56990C30895 CRC64;
MAEVNLSASL SKRSRSTDSR VSAGQCSDAS DADGKSVHGK PAIPSYLTQP AKYVRDKFSE
LEWMERHRRA AGALSQDPSH KWTLDTSPQV KARNRYGDVQ AWENCRVHLK VPDGECDFIN
ASPIVLKDPE TDGEYKYIAS QGPKRDRLAD FWNMIYHEAG EVAVLVMLTQ TVESGKEKCA
QYFPQDMENP IFEFSSPSGV AQDSENPPAA HFSGSVTLLN TSYDESIRSN VSELELRVGS
STKTVWHFLF AGWSDYGTPE GPDRDALLNL MTATAEKAKS FSNPRIVHCS AGVGRTGTFI
ALDHLLRQLR SGQLLNTNDK SADVIFNTVN RLREQRMLMV YNAFQYQFIY DVLKEQTQIK
LGIEAAPIEP RPQKIAKPDD GMFKPELVAL SPADISTADE PEDEEVEGKD KADKKNDNND
DNDGDDEEEN DDGDDEEDDE DDDEDDEDDD EEV
//
