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Database: UniProt
Entry: T1GQS4_MEGSC
LinkDB: T1GQS4_MEGSC
Original site: T1GQS4_MEGSC 
ID   T1GQS4_MEGSC            Unreviewed;       306 AA.
AC   T1GQS4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   08-NOV-2023, entry version 31.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS   Megaselia scalaris (Humpbacked fly) (Phora scalaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Platypezoidea;
OC   Phoridae; Megaseliini; Megaselia.
OX   NCBI_TaxID=36166 {ECO:0000313|EnsemblMetazoa:MESCA005988-PA, ECO:0000313|Proteomes:UP000015102};
RN   [1] {ECO:0000313|Proteomes:UP000015102}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Durham, NC isolate 2 -- Noor lab
RC   {ECO:0000313|Proteomes:UP000015102};
RA   Hughes D.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:MESCA005988-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00001490};
CC   -!- SIMILARITY: Belongs to the MPI phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00011065}.
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DR   EMBL; CAQQ02394468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1GQS4; -.
DR   STRING; 36166.T1GQS4; -.
DR   EnsemblMetazoa; MESCA005988-RA; MESCA005988-PA; MESCA005988.
DR   HOGENOM; CLU_014464_3_0_1; -.
DR   OMA; FARCNSA; -.
DR   Proteomes; UP000015102; Unassembled WGS sequence.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro.
DR   CDD; cd01530; Cdc25; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR000751; MPI_Phosphatase.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   PANTHER; PTHR10828:SF17; CDC25-LIKE PROTEIN PHOSPHATASE TWINE-RELATED; 1.
DR   PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   PRINTS; PR00716; MPIPHPHTASE.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015102}.
FT   DOMAIN          162..275
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   306 AA;  35088 MW;  DB42C7EB67529185 CRC64;
     MALEDELDAQ QLPSNLNSLI TSSIKTENHL ESPILKRPIC TKSINSLRAR SLFFEPTTPE
     LLKKEKAPES EKILPSFKKP EISKRPISVC TEKENKAPVL RKCMSMNDAE IMSALSRPTT
     EEHIGDHSKP YVLPLIKGHH NDLKSITCDT MAQLLRGEFD DKIASYKVID CRYPYEFQGG
     HIQGAVNWYN QDMILENLVN NKNLFPKDSG KGGEEQRYIL VFHCEFSSER GPKMSRFLRN
     FDRNANEYPN LQFPEIYLLH NGYKEFFKHH PNLCDPVSYL PSWTQSTAMI YVTFAQADSK
     SPSPEN
//
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