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Database: UniProt
Entry: A0A0L0DPG0_THETB
LinkDB: A0A0L0DPG0_THETB
Original site: A0A0L0DPG0_THETB 
ID   A0A0L0DPG0_THETB        Unreviewed;       613 AA.
AC   A0A0L0DPG0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=AMSG_09550 {ECO:0000313|EMBL:KNC53911.1};
OS   Thecamonas trahens ATCC 50062.
OC   Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX   NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC53911.1, ECO:0000313|Proteomes:UP000054408};
RN   [1] {ECO:0000313|EMBL:KNC53911.1, ECO:0000313|Proteomes:UP000054408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC53911.1,
RC   ECO:0000313|Proteomes:UP000054408};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA   Ruiz-Trillo I., Lander E., Nusbaum C.;
RT   "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004273};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273}.
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DR   EMBL; GL349484; KNC53911.1; -; Genomic_DNA.
DR   RefSeq; XP_013754117.1; XM_013898663.1.
DR   AlphaFoldDB; A0A0L0DPG0; -.
DR   STRING; 461836.A0A0L0DPG0; -.
DR   EnsemblProtists; KNC53911; KNC53911; AMSG_09550.
DR   GeneID; 25567988; -.
DR   eggNOG; KOG0375; Eukaryota.
DR   OrthoDB; 1488111at2759; -.
DR   Proteomes; UP000054408; Unassembled WGS sequence.
DR   GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:InterPro.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0097720; P:calcineurin-mediated signaling; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
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:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT 1-RELATED; 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   Hydrolase {ECO:0000256|RuleBase:RU004273};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054408}.
FT   DOMAIN          174..179
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  67493 MW;  0732D322C5584D0D CRC64;
     MSSAGASSRR SRERSTSRSR SASPKLAAIV DRYDIPEDTA VRMCTVVPAP RRPAMSADEL
     FSGPGGDVNT DLLLQHLRTE GRLSLEAASQ LLETAREVLS REPNCVPLEA PMHIVGDIHG
     QFYDLLHMFD SLGLPPKRKY LFLGDYVDRG IYSTEVAILL LGLKIRYPEH VTLIRGNHES
     RAMAAYHSMK TETLYKYSET TYNEFMEAFD ALPVAATVAG PAGTFLCVHG GLSPAVNTIE
     AINALARFGE VPASGPLCDL MWSDPVPDAT ATGLSGSQLR QWKEITFEFN EQRGCSYRYG
     RRAVRDFLTA NGLVGIIRAH EVQENGYNEH RFREEAEDDP LSPFPLVTTV FSAPNYCEMY
     DNSAAVALYD GTTLEFVSYE CVEHPFGLPD YMDSLNWSLP YVMEKVTQFF AVSLKLIEGD
     SDSDSDDDEP MQTDAGPASP VSRKASAKAL RDAARAAAAR KRANQKAAAE APEPATAPDT
     AASEPPASSA AASAAGTPGS SADDASAPEG DDAAAFRSRT SRVRTRKRPA MRQRSSSNIC
     NETIRTRRAS MNTLLRRAEK LRERNMRLLV AANDDDDDDD DDAADDTLSR FERALRKDSK
     REYLRPLQRH YTM
//
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