GenomeNet

Database: UniProt
Entry: A0A182PIY7_9DIPT
LinkDB: A0A182PIY7_9DIPT
Original site: A0A182PIY7_9DIPT 
ID   A0A182PIY7_9DIPT        Unreviewed;       639 AA.
AC   A0A182PIY7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS   Anopheles epiroticus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI006900-PA, ECO:0000313|Proteomes:UP000075885};
RN   [1] {ECO:0000313|Proteomes:UP000075885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AEPI006900-PA}
RP   IDENTIFICATION.
RC   STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI006900-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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}.
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   AlphaFoldDB; A0A182PIY7; -.
DR   STRING; 199890.A0A182PIY7; -.
DR   EnsemblMetazoa; AEPI006900-RA; AEPI006900-PA; AEPI006900.
DR   VEuPathDB; VectorBase:AEPI006900; -.
DR   OrthoDB; 12481at2759; -.
DR   Proteomes; UP000075885; 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}.
FT   DOMAIN          460..580
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   639 AA;  70462 MW;  537918ECCEF56105 CRC64;
     MFRFTLNSAG RSPASRRAEQ RQRSLQFRQH GMPQRMIYDD GCKLLGSPGK ENLPTEELSF
     YQSHSPQQSP RPCSPCTLCP EDGELLPSES NTPSKHMTIP ILNRSGTGAI VAGKLLTTTT
     TTVPGGLGYR LRRPLDDHDP NSMDSGYGAS VLSDALMNSL HSSAGSVTST KPHCSIFPFN
     QSAVTAMSRH SSTSSPASTR GRLLLQHSSL SSGSMESMDD MELFDMETME EDDAMEEGCR
     MQAGDRAQTQ RPSGLSSLIC GTIKTTRTAT TPEQQKRPFV RRCLSLTEHN HNVLNAQQQM
     KTPERYSRRM IAMEDQENCN LTPYSSRTAA SATEVTRCFK RPEPPGISPV QSKRSKTQAD
     SGPFSPSPAV PPPTAALDSP ARTTVLAAAA MPKKLVYQKS ISMNDAQIMS ALSRSSSEPD
     LIGDFSKSYV LPLMEGQHRD LKSISGDTMA RLLRGDYSDK IASFKIIDCR YPYEYEGGHI
     RGAKNLYTQE QIVDELIKSK TEPPAVSDGS SAQDGGATRR HIIVFHCEFS SERGPKLSRF
     LRNHDRTLNA DSYPALHYPE MYLLHGGYKE FFKAHAELCD PIAYRPMLDP EYGEAYRHFR
     AKSRSWNGDG TGTIKATVTS STLAGGPSRL TKSRSRLML
//
DBGET integrated database retrieval system