ID E1F325_GIAIA Unreviewed; 726 AA.
AC E1F325;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=GLP15_1007 {ECO:0000313|EMBL:EFO63169.1};
OS Giardia intestinalis (strain P15) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=658858 {ECO:0000313|EMBL:EFO63169.1, ECO:0000313|Proteomes:UP000008974};
RN [1] {ECO:0000313|EMBL:EFO63169.1, ECO:0000313|Proteomes:UP000008974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P15 {ECO:0000313|EMBL:EFO63169.1,
RC ECO:0000313|Proteomes:UP000008974};
RX PubMed=20929575; DOI=10.1186/1471-2164-11-543;
RA Jerlstrom-Hultqvist J., Franzen O., Ankarklev J., Xu F., Nohynkova E.,
RA Andersson J.O., Svard S.G., Andersson B.;
RT "Genome analysis and comparative genomics of a Giardia intestinalis
RT assemblage E isolate.";
RL BMC Genomics 11:543-543(2010).
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|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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:EFO63169.1}.
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DR EMBL; ACVC01000142; EFO63169.1; -; Genomic_DNA.
DR AlphaFoldDB; E1F325; -.
DR STRING; 658858.E1F325; -.
DR EnsemblProtists; EFO63169; EFO63169; GLP15_1007.
DR VEuPathDB; GiardiaDB:GLP15_1007; -.
DR OMA; AVINDRY; -.
DR OrthoDB; 5475990at2759; -.
DR Proteomes; UP000008974; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR Pfam; PF00149; Metallophos; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 255..260
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
SQ SEQUENCE 726 AA; 81610 MW; FFE6E86A4904240D CRC64;
MGRKSRSHKD YGKTKRTGTI DLSSMTSFTS YTNSPLPRAD LERRKKLFFS NPKQQNSPPT
EKEVRNFAYK ITEDWFNSIA KDIRKTFVTK KVGGSVQETV DLKEILPISF VREVLTLGTR
VLASCPNILE LTVPPTELKS FKKKLPAEYS KNLLKSCTNL SEIQSISPSV LEDLGPIDME
CSSVVLPCKR LVVVGDTHGT FEVIEKILTT EGFPTDNEIV YLFNGDYVDR GSFSIEIFIV
LLAIKIAKPD AVHLLRGNHE TESVNSNYSL PAEIEKKYGK ALGEEECKIL LTMMNKAFQA
LPLCAVINDR YLVVHGGISA WPDFTLQDIA KLNRFREPDQ ADFTNYTYFD PLSDILWADP
GTEDPEFSFN YLRGTSIIFG AVAAQRFLRT SELKYIIRSH SCVDEGWQVE YPGVFTLFSV
PNYAEKNLGA YAVFYGLYDK TEELSSLDKE VLKEDATPKA KYNLSPSEPL VFIKKFTCSQ
HSAMVNQPLL SDGPSSFFEV PEEDSIDICT IIKNNEEMKM NLLAQVIEDP EQCLVAVPEK
GGVVVPHLIG ATIGTRIHQD KNSNIRLKQR IIETAEKIPI PDSIPTDDLV EALVLLTDIM
TLTTPAVIGA FPHELQAKLL HIPFDNDSYS LEELGLAIPG STFPPVLPVE VIKIVLSCLT
DPLKRDSNWL EEAGARKAMQ IFRRFHDFDV PISKADKFLL QLTKTARSPP FLPLFSKPFR
YAKLKY
//
