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Database: UniProt
Entry: A0A3B3XBA5_9TELE
LinkDB: A0A3B3XBA5_9TELE
Original site: A0A3B3XBA5_9TELE 
ID   A0A3B3XBA5_9TELE        Unreviewed;       680 AA.
AC   A0A3B3XBA5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000012244.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000012244.1}
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   RefSeq; XP_014840782.1; XM_014985296.1.
DR   RefSeq; XP_014840784.1; XM_014985298.1.
DR   RefSeq; XP_014840785.1; XM_014985299.1.
DR   AlphaFoldDB; A0A3B3XBA5; -.
DR   STRING; 48701.ENSPMEP00000012244; -.
DR   Ensembl; ENSPMET00000019618.1; ENSPMEP00000012244.1; ENSPMEG00000014405.1.
DR   GeneID; 106916780; -.
DR   KEGG; pmei:106916780; -.
DR   CTD; 393854; -.
DR   OrthoDB; 2901840at2759; -.
DR   Proteomes; UP000261480; 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; cd14645; DSP_DUSP8; 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; IPR048035; DUSP8_DSP.
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:SF108; DUAL SPECIFICITY PROTEIN PHOSPHATASE 8; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF00581; Rhodanese; 1.
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          25..140
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   DOMAIN          162..304
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          224..285
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          341..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..663
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   680 AA;  73521 MW;  5D317C2058A53407 CRC64;
     MAGEKAPNKR SAMDIKRLAS LIQRGTGRLL VIDSRTFSEY NASHVQGAVN VCYSKLVKRR
     LQQDKVSVTE LLQPNGKVKV ELGRKQEVVV YDQSSKEAGH LSKDGFVHIL MGKLEGTFHK
     VSLLTGGFAA FSSCFPGLCE GKPATALPMS LSQPCLPVAN VGPTRILPHL YLGSQKDVLN
     KDLMSQNGIT YVLNASNTCP KPDFISESHF MRIPVNDNYC EKLLPWLDKT NEFIDKAKVS
     NCRVIVHCLA GISRSATIAI AYIMKTMGLS SDDAYRFVKD RRPSISPNFN FLGQLLEFEK
     GLRLLQALTT DDKKSENNSK QSSEVNGVSA GFEINGHHTS CDSSVADPHA QTEPKLPSPT
     SLQQGFNGLH LSAERIMDTN RLKRSFSLDI KSVYSLSSPH CPSMAPTHSE DIPKLCKLDS
     PGTGTSNGVC SQSPVLHSPG SFDSPFPSPS SGGSIGGLGG SEGVHRSGTS SSRSRRKTKH
     NCGSSPVHSH LQHPPQSLSL SLDHKSPSLE ENLRGSPLLS LPSLPSLGSG AMWTKHRDTV
     QATTPVTPVT PTMDAPWHFG ADEGGEGEME LGGGDGRGEE SSVRFGSSSA YVAFGCSEGA
     RLRDKSQREK LSGPQTQRDH WDSTSASSSN GVPASEKQFK RRSCQMEFEE GISETRSREE
     LGKIGKQSSF SGSMEIIEVS
//
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