ID A0A1Y1S571_9MICR Unreviewed; 424 AA.
AC A0A1Y1S571;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=FCP1 {ECO:0000313|EMBL:ORD93539.1};
GN ORFNames=ECANGB1_2032 {ECO:0000313|EMBL:ORD93539.1};
OS Enterospora canceri.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterospora.
OX NCBI_TaxID=1081671 {ECO:0000313|EMBL:ORD93539.1, ECO:0000313|Proteomes:UP000192639};
RN [1] {ECO:0000313|EMBL:ORD93539.1, ECO:0000313|Proteomes:UP000192639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB1 {ECO:0000313|EMBL:ORD93539.1,
RC ECO:0000313|Proteomes:UP000192639};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:ORD93539.1}.
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DR EMBL; LWDP01000070; ORD93539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1S571; -.
DR VEuPathDB; MicrosporidiaDB:ECANGB1_2032; -.
DR Proteomes; UP000192639; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR PANTHER; PTHR23081:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000192639}.
FT DOMAIN 87..240
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
SQ SEQUENCE 424 AA; 49575 MW; 0F390C1451D2BDFE CRC64;
MDDPGGNPKR TKKTAALDDL EKEIDFELDM QDEKCSHALR MGDLCANCGT CLERDVNLVT
VTHGSDQLLQ RYEDAFRSHL KHFYKLAEHR KLILLCDLDQ TVIHATLEKA NCDFSFELDG
VRFAVKNRRW LDQFLRKTNR LFEMHVYTLG TRGYADAVCK AIDPDKTYFG DRIVTRTENN
NELKKYIKRI TSFDQNVLVL DDRIDVWGFI PNCIFIRPFC YYSMEDVNDP VRLAKMRLAA
KKENFLDAAI QRLLDEEAQS NQDRAADEYR SMVKEDVNVE IEEESEGEED IFDISNKPNK
EDMELKKVYL ILKKLHKGYF RKLDRIRKNE RVEDIPVEQL INVGDVAQIR ALKRYSVVCR
SKYRNYVLYL GGRIIKIADL EHEDKSRILV INDRAVASKY GIRNMSEDLL TACLYNRCFV
TRDT
//
