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Database: UniProt
Entry: A0A3B3U9D6_9TELE
LinkDB: A0A3B3U9D6_9TELE
Original site: A0A3B3U9D6_9TELE 
ID   A0A3B3U9D6_9TELE        Unreviewed;       514 AA.
AC   A0A3B3U9D6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000009935.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000009935.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001512};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001482,
CC         ECO:0000256|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000256|ARBA:ARBA00001965};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.
CC       {ECO:0000256|ARBA:ARBA00009905}.
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DR   RefSeq; XP_014887306.1; XM_015031820.1.
DR   AlphaFoldDB; A0A3B3U9D6; -.
DR   STRING; 48699.ENSPLAP00000009935; -.
DR   Ensembl; ENSPLAT00000000366.1; ENSPLAP00000009935.1; ENSPLAG00000012804.1.
DR   GeneID; 106947041; -.
DR   KEGG; plai:106947041; -.
DR   CTD; 565241; -.
DR   GeneTree; ENSGT00940000154115; -.
DR   OrthoDB; 1488111at2759; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IEA:InterPro.
DR   CDD; cd07416; MPP_PP2B; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041751; MPP_PP2B.
DR   InterPro; IPR043360; PP2B.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45673; SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 1.
DR   PANTHER; PTHR45673:SF2; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT GAMMA ISOFORM; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          144..149
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          472..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  57888 MW;  06DBAA5D985F94E0 CRC64;
     MSTKDQNKLS TVERPIKAVP YPPGTRLSVK DLYADGKPSL ELLKAHLVKE GRLEEEAALR
     IINEGASILR KEKCMLEVEA PITVCGDVHG QFFDLMKLFE VGGSPSNTRY LFLGDYVDRG
     YFSIECVLYL WALKINYPDT LFLLRGNHEC RHLTEYFTFK QECKIKYSEQ VYDACMEAFD
     CLPLAALLNQ QFLCVHGGLS PEITCLDDIR KLDRFKEPPA FGPMCDLLWS DPGEDYGSEK
     TQEHFSHNSV RGCSYFYSYP AVCDFLMNNN LLSVIRAHEA QDAGYRMYRK SQTTGFPSLI
     TIFSAPNYLD VYNNKAAVLK YENNVMNIRQ FNCSPHPYWL PNFMDVFTWS LPFVGEKVTE
     MLVNVLNICS DDELMSEGDD TCEGGAPAAR KEVIRNKIRA IGKMARVFSV LREENESVLQ
     LKGLTPTGTL PLGVLSGGRR TLQSATVEAE EARAIQGFNP QHKIQSFEEA RGLDLINERM
     PPRRDSKQNE GPPSFNNLPA GTGPPDKNGT NAQA
//
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