ID   A0A3B5BCJ7_9TELE        Unreviewed;       478 AA.
AC   A0A3B5BCJ7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000030785.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000030785.1}
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   AlphaFoldDB; A0A3B5BCJ7; -.
DR   STRING; 144197.ENSSPAP00000030785; -.
DR   Ensembl; ENSSPAT00000031282.1; ENSSPAP00000030785.1; ENSSPAG00000023101.1.
DR   GeneTree; ENSGT00940000165110; -.
DR   Proteomes; UP000261400; 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:SF3; SERINE_THREONINE-PROTEIN PHOSPHATASE; 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          117..122
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          444..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  54061 MW;  D56F556895D77FC8 CRC64;
     MKEVFDSEGK PRVDLLKAHL TKEGRVEEAV ALRIVNEGAA ILRQEKTILD IEAPVTVCGD
     IHGQFFDLMK LFEVGGSPAT TRYLFLGDYV DRGYFSIECV LYLWSLKILY PKTLFLLRGN
     HECRHLTEYF TFKQECKIKY SEQVYDSCMD AFDCLPLAAL MNQQFLCVHG GLSPEIHTLD
     DIKKLDRFKE PPAFGPMCDL LWSDPLEDFG NEKTQEYFSH NTVRGCSYFY SYPAVCEFLQ
     SNNLLSIIRA HEAQDAGYRM YRKSQTTGFP SLITIFSAPN YLDVYNNKGQ KNLFISSVFD
     LVCGFISDLS WSINFFTEML VNVLSICSDD ELMNDEDEIF DANAAAARKE VIKNKIRAIG
     KMAKMFSVLR EESENVLTLK GLTPTGMLPS GVLSGGRQTL QSATIEAIEA IETHDEDREA
     IRGFSPQHKI TSFEEAKGLD RINERMPPRK DGVNHVGHSM GKMNMSEANG TEDNSNVQ
//