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Database: UniProt
Entry: A0A3Q1F8C9_9TELE
LinkDB: A0A3Q1F8C9_9TELE
Original site: A0A3Q1F8C9_9TELE 
ID   A0A3Q1F8C9_9TELE        Unreviewed;       849 AA.
AC   A0A3Q1F8C9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000014016.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000014016.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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};
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DR   AlphaFoldDB; A0A3Q1F8C9; -.
DR   STRING; 80966.ENSAPOP00000014016; -.
DR   Ensembl; ENSAPOT00000022325.1; ENSAPOP00000014016.1; ENSAPOG00000016860.1.
DR   GeneTree; ENSGT01040000240451; -.
DR   InParanoid; A0A3Q1F8C9; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR011948; Dullard_phosphatase.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
DR   NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR   PANTHER; PTHR12210:SF139; CARBOXY-TERMINAL DOMAIN RNA POLYMERASE II POLYPEPTIDE A SMALL PHOSPHATASE 1; 1.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT   DOMAIN          674..832
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   REGION          72..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..116
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..399
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            740
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
FT   SITE            778
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
SQ   SEQUENCE   849 AA;  95867 MW;  0AD15CBFE9914B81 CRC64;
     MPTDQQSESS DFEPDELEVS CGSFGQYEMS NLGPECTEHL QYELSHQQCE SFDSEPDTST
     EDFEQCEMSI ISDSGDSLDC GGEYCEYDEN QNQTECTNND DDDDDDSYEG EQNELEPSDE
     ESSRSAEDSE DSPCVGDFFE THVYTKENSQ QVSTSDMSAD PSELCGNDNS ETSQEFEPTH
     QSERNYENSF CSEEDGSSDC SSVETKSFKT CPDGSIPCDP CSDSSGESEK GAQEDSSDEQ
     TQWESFEEDE EIQQSSINKS NEDQQKTPSV DIVIEDYFDL FDRADYHRHM FAQKQRYISC
     FDGGDIHDHL YLEEEAQMHK AKNMYKSEEV NEEINVPQTD VCSEDAHEES SEEDTGQRDE
     EWIGQSESSL TGDEDEENEA ETLASYTENS DEAEDDEAHF DEEPCALDVS EVCNEEDEAC
     LSTGNEESMC APCAKEISVE GDAYEEEVYD TQEKYESLGG VTCTSDETEL TAADDKDEPA
     PEDDVFIACS EMEPYWSLID DEEIGEFCEL DVEDYYAYQI KSIQSSIQQA LNGFIVGERS
     YDASRNKRKD ALVSLEEEQA NPQECKTVTF QITEVIELNC SVVEETVDED CMLNEGSRQL
     KLPSDIIHSV SKHAKIEGGD VAVKRTEDNK ASEQTRHSEE ESDDESCELC ECDYCIPPTE
     QVPTQPLLPQ MKSNDAGKIC VVIDLDETLV HSSFKPVNNA DFIIPVEIDG TVHQVYVLKR
     PHVDEFLKRM GELFECVLFT ASLSKYADPV SDLLDKWGAF RSRLFRESCV FHKGNYVKDL
     SRLGRDLNKV IIIDNSPASY VFHPDNAVPV ASWFDDMSDT ELLDLIPFFE RLSKVDDIYE
     ILKQQRTSS
//
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