ID A0A0N4SXW2_BRUPA Unreviewed; 323 AA.
AC A0A0N4SXW2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=BPAG_LOCUS538 {ECO:0000313|EMBL:VDN81724.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000053701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0000053701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN81724.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR EMBL; UZAD01000025; VDN81724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4SXW2; -.
DR STRING; 6280.A0A0N4SXW2; -.
DR WBParaSite; BPAG_0000053701-mRNA-1; BPAG_0000053701-mRNA-1; BPAG_0000053701.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; Unassembled WGS sequence.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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:SF398; SERINE/THREONINE-PROTEIN PHOSPHATASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000278627}.
FT DOMAIN 118..123
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
SQ SEQUENCE 323 AA; 36403 MW; 2967B751EF159092 CRC64;
MSEININDLI LRLLNVGQPA KGLTKTVREP EIASLCRKAR DIFIAQPSLI EIDPPVRICG
DTHGQYGDLL RIFGRGGFPP LANYLFLGDY IDRGHQNLET IILLFCYKVK FPNNFFLLRG
NHECANVNRV YGFYEECIRR FNSVHLWQIF QFRFSKRLSL QDTFQCMPLT ALVGERILCM
HGGISPQLKS LQQLREIKRP VDITSPSLEM DLLWADPVIG ISGFQMNMRG ASFGFGADIL
AALCKELNID MVARAHQVVQ DGYEFFGGRK CVTIFSAPHY CGQFDNAAAV MSVDQNLLCS
FQILRPTIGR ATARIIPTSM GKC
//