ID Q4U9P3_THEAN Unreviewed; 795 AA.
AC Q4U9P3;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=TA08350 {ECO:0000313|EMBL:CAI76460.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI76460.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI76460.1, ECO:0000313|Proteomes:UP000001950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
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 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. BSU subfamily.
CC {ECO:0000256|ARBA:ARBA00005671}.
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DR EMBL; CR940353; CAI76460.1; -; Genomic_DNA.
DR RefSeq; XP_953085.1; XM_947992.1.
DR AlphaFoldDB; Q4U9P3; -.
DR STRING; 5874.Q4U9P3; -.
DR GeneID; 3863045; -.
DR KEGG; tan:TA08350; -.
DR VEuPathDB; PiroplasmaDB:TA08350; -.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR InParanoid; Q4U9P3; -.
DR OMA; CKEGPAT; -.
DR OrthoDB; 311640at2759; -.
DR Proteomes; UP000001950; Chromosome 4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR012391; Ser/Thr_prot_Pase_BSU1.
DR PANTHER; PTHR46422; SERINE/THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR PANTHER; PTHR46422:SF4; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036363; PPP_BSU1; 2.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF117281; Kelch motif; 2.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001950};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 101..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 561..566
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 767..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 89892 MW; 67642DD46C67CE9A CRC64;
MAYLKVVPQQ GDVPPPRFGH TTTSVGSGKV VLFGGAVGDV GRYTITSDSF LYDVTTNHWT
KLQTENPPSP RAAHAAACVE TMQVVIFGGA TGGGALSSDD VLNYIPILIY IAMYILFLLD
LRRDKQLSWI IVPTTGRSPG RRYGHTMVFS KPNLILIGGN DGQMPSNDVW VLNVEQSPFS
WNEVTFSPTI QLPPIRVYHS SDLCCEGPAN GMIVIFGGRG NESKSLNDLW GLRQHRDGTW
DWIEAPINSG NKPDPRYQHY NSIDSIDNSI TCSFVGSKFV ILGGRSDSDL NKSLSISVYD
TETLEWFNIS TIQRFRHSSW RFGPNLYIFG GFANQTQKHP TCELKILDCQ KNGNTGVLFQ
SSPKTREEFR KPQDREIRLS AHAHAVRESV SDFSYLVRKI SIDRLEEEGR KINKPEARSS
LHWQNENPDT IYDRIIMKLL NPNELKFQKD SSFSISYKDI NTLLNTVYHI IKEEETVLNL
RAPIKIYGDI HGQYHDLTRL FKLYKSPLDE YLAEALCLEG DIESNDYLFL GDYVDRGFNS
LEVICLLFAL KCKYPAQIHL IRGNHEDPAI NAVYGFQNEC ARRLNEDVDN PFSCWNAFNK
IFELLPLGAI IEGRILCVHG GIGKSIERID DIRSLKRPIS VIPIPESPED QLLLDLLWSD
PTDNDSMLGT VPNEIRDPDR AGFIVKFGPD RVLKFLTNND LQLIIRAHEC VMDGFERFAG
GRLITLFSAT NYCNHHKNAG ALLFIRRDLT IVPKLIYPSQ DETSYDSWDM RMSDTRPPTP
PRSTPMARDM IIEPA
//
