ID A0A3B0K0A8_DROGU Unreviewed; 327 AA.
AC A0A3B0K0A8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=DGUA_6G007384 {ECO:0000313|EMBL:SPP76798.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP76798.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-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};
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DR EMBL; OUUW01000002; SPP76798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0K0A8; -.
DR STRING; 7266.A0A3B0K0A8; -.
DR OMA; LFCCWRN; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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 InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR040078; RNA_Pol_CTD_Phosphatase.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR12210:SF171; PHOSPHATASE HERZOG; 1.
DR Pfam; PF03031; NIF; 1.
DR SFLD; SFLDG01124; C0.1:_RNA_Pol_CTD_Phosphatase; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Ribonucleoprotein {ECO:0000313|EMBL:SPP76798.1};
KW Ribosomal protein {ECO:0000313|EMBL:SPP76798.1}.
FT DOMAIN 85..243
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 262..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 151
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
FT SITE 189
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR640078-3"
SQ SEQUENCE 327 AA; 37537 MW; 18255CB2834120A9 CRC64;
MDATSIITQV SRDDEQLNVY PSYPNDKDDV ERLKPQKRGF IQSLLCCWRR NRTKTNQNGT
QIDGSTTPPP LQDQQRYLLP QVRLTDVHRK CMVIDLDETL VHSSFKPIPN ADFIVPVEID
GTVHQVYVLK RPHVDEFLQK MGELYECVLF TASLAKYADP VADLLDKWNV FRARLFRESC
VYYRGNYIKD LNRLGRDLQK IVIVDNSPAS YIFHPDNAVP VKSWFDDVTD CELRELIPLF
EKLSKVDSVY SVLCNSNQPL NNHQSNQLQQ HPQELQQAPN QLQQQQQQQT ISATTVITQA
TTLSAPTMLQ QQSPSPPSPQ SELLQKT
//