ID A0A3B4V9W2_SERDU Unreviewed; 692 AA.
AC A0A3B4V9W2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000027429.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000027429.1}
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; A0A3B4V9W2; -.
DR STRING; 41447.ENSSDUP00000027429; -.
DR Ensembl; ENSSDUT00000027913.1; ENSSDUP00000027429.1; ENSSDUG00000019851.1.
DR GeneTree; ENSGT00940000160004; -.
DR OMA; DSCFHNV; -.
DR OrthoDB; 2901840at2759; -.
DR Proteomes; UP000261420; 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 344..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 74605 MW; 0C9C752F46B25688 CRC64;
MAGEKGPTKR STMDIKRLAS LIQRGTGRLL VIDSRTFSEY NASHVQGAVN VCCSKLVKRR
LQQDKVSVTE LLQPNGKVKV ELGRKQEVVV YDQSSKEAGH LSKDGFVHIL MGKLEGTFHK
VSLLTGGFAA FSSCFPGLCE GKPATALPMS LSQPCLPVAN VGPTRILPHL YLGSQKDVLN
KDLMAQNGIT YVLNASNTCP KPDFICESHF MRIPVNDNYC EKLLPWLDKT NEFIDKAKVS
NCRVIVHCLA GISRSATIAI AYIMKTMGLS SDDAYRFVKD RRPSISPNFN FLGQLLEFEK
GLRLLQALTS TSDDKISENN TKQSSEVNGV NTGFEINGLH SNYDSSVAEP HIPPEPKLPS
PTSLQQGFNG LHLSAERIMD TNRLKRSFSL DIKSVYSPNS PHCPSLAPTH SEDVPKLCKL
DSPGTGTSNG VCSQSPVLDS PSSSDSPFPS PGSGGSIGGL GLGGSEGVHR SSSSSSRPRR
KPKHSSSSSP VHPHPHQPPQ SLCLSLDHKS PSLDENLKGS LLLSLPSLPT VGSGAMWTKH
RDTVQATTPV TPVTPTTDAP WHFGAEEGGE RGMELGGGGD GGGEESSVRF GSSSAYVAFG
CSEGVRLRDK SQREKPSMPQ MQRDHRDSTS SSTVSMSNSS NNSGTASEKQ FKRRSCQMEF
EEGIAETRSR EELGKIGKQS SFSGSMEIIE VS
//
