ID A0A1J5WYA6_9MICR Unreviewed; 306 AA.
AC A0A1J5WYA6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=A8A55_1422 {ECO:0000313|EMBL:OIR57809.1};
OS Amphiamblys sp. WSBS2006.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Amphiacanthidae;
OC Amphiamblys.
OX NCBI_TaxID=1866961 {ECO:0000313|EMBL:OIR57809.1, ECO:0000313|Proteomes:UP000182028};
RN [1] {ECO:0000313|EMBL:OIR57809.1, ECO:0000313|Proteomes:UP000182028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSBS2006 {ECO:0000313|EMBL:OIR57809.1};
RX PubMed=27694476;
RA Mikhailov K.V., Simdyanov T.G., Aleoshin V.V.;
RT "Genomic survey of a hyperparasitic microsporidian Amphiamblys sp.
RT (Metchnikovellidae).";
RL Genome Biol. Evol. 0:0-0(2016).
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC {ECO:0000256|ARBA:ARBA00034714}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIR57809.1}.
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DR EMBL; MKPU01000057; OIR57809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5WYA6; -.
DR VEuPathDB; MicrosporidiaDB:A8A55_1422; -.
DR Proteomes; UP000182028; Unassembled WGS sequence.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR047129; PPA2-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR PANTHER; PTHR45619:SF12; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000182028}.
FT DOMAIN 20..290
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|SMART:SM00156"
SQ SEQUENCE 306 AA; 34484 MW; 76BFD0D0D2E43B63 CRC64;
MDSADDPARW IESLEQGRLL SEETIARLCA KAQEILAEEE NTKTLHSPVT VCGDIHGQFQ
DLREIFQITG PVPDTSYLFL GDYVDRGYNS VECICLLLTY KIAFPSKIAL LRGNHDSRQI
TQVYGFYDEC MAKYGTSRVW RLLTDLFDYL PITALIDNEV FCVHGGLSPD ITEISGVSSI
NRVVEIPHDG PMCDLLWSDP DEKPGWNLSP RGAGYFFGPD VTREFNHRNN TKLIARAHQL
VMNGYSFAHN NEVVTLFSAP NYCYRCGNMA AVMELDQGSV SRLTQYDSAP NATELKITKR
LAEYFL
//
