ID A0A182M4D9_9DIPT Unreviewed; 300 AA.
AC A0A182M4D9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
OS Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA009189-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|EnsemblMetazoa:ACUA009189-PA, ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA009189-PA,
RC ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA009189-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA009189-PA};
RG VectorBase;
RL Submitted (OCT-2016) to UniProtKB.
RN [3] {ECO:0000313|EnsemblMetazoa:ACUA009189-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA009189-PA};
RG EnsemblMetazoa;
RL Submitted (JAN-2021) 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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR EMBL; AXCM01000266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182M4D9; -.
DR STRING; 139723.A0A182M4D9; -.
DR EnsemblMetazoa; ACUA009189-RA; ACUA009189-PA; ACUA009189.
DR VEuPathDB; VectorBase:ACUA009189; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000075883; Unassembled WGS sequence.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07414; MPP_PP1_PPKL; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF472; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-BETA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}.
FT DOMAIN 92..97
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 273..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 34571 MW; 22E62E4743C06948 CRC64;
MPEEEIRALC LKSREIFLQQ PILLELEAPL KICGDIHGQY TDLLRLFEYG GFPPEANYLF
LGDYVDRGKQ SLETICLLLA YKIKYPENFF LLRGNHECAS INRIYGFYDE CKRRYNVKLW
KTFTDCFNCL PIAAIIDEKI FCCHGGLSPD LNHMEQIKRI MRPTDVPDTG LLCDLLWSDP
DKDVKGWGEN DRGVSFTFGV DIVAKFLLIH ELDLICRAHQ VVEDGYEFFA RRSLVTLFSA
PNYCGEFDNA GGMMSVDANL MCSFQILKPS EKKAKYQYSG TNNQRPQTPQ RNQNPTNKRK
//
