ID A0A3B4BAG4_9GOBI Unreviewed; 472 AA.
AC A0A3B4BAG4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000025915.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000025915.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601}.
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DR AlphaFoldDB; A0A3B4BAG4; -.
DR STRING; 409849.ENSPMGP00000025915; -.
DR Ensembl; ENSPMGT00000027601.1; ENSPMGP00000025915.1; ENSPMGG00000020894.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14567; DSP_DUSP10; 1.
DR CDD; cd01446; DSP_MapKP; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF299; DUAL SPECIFICITY PROTEIN PHOSPHATASE 10; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR01908; ADSPHPHTASE.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 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; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 166..283
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 311..454
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 374..433
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 85..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 52067 MW; 44D62DDFF14A7511 CRC64;
MPPSPLDDRI VVALPRPSRP QELTLSLDSS YLDTFSSAEH TVISTTVVTI RATYMPSSKG
STRSLSCGCS SASCCSVTTY ERDSPSLSHS SPNLSYAGTP SPQLPPLRSH EARSVPSLAS
GLAPSTPKAL PRALPTALPK LLPSVRLMHP NELAKRLSCC PLGHPVGPVP VIIDCRPFTE
YNKSHIRGAV HINCSDKMSR RRLQQGKITV LDLLSCREAQ DSFKGLFSKD IVVYDDSTMD
PHRLSPAQPL HVVLESLRRE GKDPMVLKGG LSCFRMSHED LCEHSLHLDD GLDPCASSSG
LTGALPHSLM PITPILPSLY LGNEQDAQDL RLLQRLNVGY ILNVTTHLPL YHYDTGLFVY
KRLPATDSNK QNLRQYFEEA FEFIEEAQQA GMGLLIHCQA GVSRSATIVI AYLMKHTWMT
MTDAYKYVKT RRPIISPNLN FMGQLLEFEE DLNNGITPRI LAPKLMGVET IV
//
