ID M2W254_GALSU Unreviewed; 356 AA.
AC M2W254;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=Gasu_27740 {ECO:0000313|EMBL:EME29771.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME29771.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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 -!- SIMILARITY: Belongs to the dullard family.
CC {ECO:0000256|ARBA:ARBA00038346}.
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DR EMBL; KB454505; EME29771.1; -; Genomic_DNA.
DR RefSeq; XP_005706291.1; XM_005706234.1.
DR AlphaFoldDB; M2W254; -.
DR STRING; 130081.M2W254; -.
DR EnsemblPlants; EME29771; EME29771; Gasu_27740.
DR GeneID; 17088542; -.
DR Gramene; EME29771; EME29771; Gasu_27740.
DR eggNOG; KOG1605; Eukaryota.
DR OMA; VNIRVIY; -.
DR OrthoDB; 1558at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016791; F: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 NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210:SF70; CTD NUCLEAR ENVELOPE PHOSPHATASE 1; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 166..324
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
SQ SEQUENCE 356 AA; 41146 MW; F5918DD999BC7E70 CRC64;
MNSYKQRQSK TESVGAHISV APAERTSTDK SKLSVLGHTA LQLVNSLYSS LCESINRFLF
LHWWRRKSRE NSHITTAGKR SARDVTSPVL FFVNIRVIYK ILLPFTLFLP IVSLLLGLLR
ELLSSALNSI FQGFRLVLFS HNHLRMLYCS LFDIWNPEQS EKEQIFYHGR KTLVLDLDET
LVHSTTRQNS HFDIRLEVSV DNCPSIFYVN KRPYLDVFLR VVSQWYDLVV YTASLQKYAD
PLIDALDVHG VIRERYFRDH CIQVGNNFVK DISIIEPDLR KIVIVDNSPS AYVLHEENAI
PIGTWWDDPL DEELLNLLPF LQALCVLADV RSILSLRETK GVLLHHLISS RPYHTL
//
