ID U6L1E2_EIMTE Unreviewed; 895 AA.
AC U6L1E2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=ETH_00020760 {ECO:0000313|EMBL:CDJ42404.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ42404.1};
RN [1] {ECO:0000313|EMBL:CDJ42404.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ42404.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ42404.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ42404.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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};
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}.
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DR EMBL; HG675716; CDJ42404.1; -; Genomic_DNA.
DR RefSeq; XP_013233154.1; XM_013377700.1.
DR AlphaFoldDB; U6L1E2; -.
DR EnsemblProtists; CDJ42404; CDJ42404; ETH_00020760.
DR GeneID; 25253270; -.
DR VEuPathDB; ToxoDB:ETH2_1126900; -.
DR VEuPathDB; ToxoDB:ETH_00020760; -.
DR OrthoDB; 227228at2759; -.
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; 3.40.50.10190; BRCT domain; 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; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 398..578
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 645..732
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 98379 MW; F58EB4E3EF57F4BC CRC64;
MRDGFRGRGR GRGGGGWRGS QRATIAESHE QQWKSGLGLV PGQESRHFNP REARARPERE
AEPPHGSVPM HSTAPHRRRH QGQGLRKERA APYEARAGLL PHGVPPGAAR VPPLGLGGRV
GAMEVVDGQL ACAAPLQGCS MPAVCCSVYA DQIIDYYTGR ICPRRFCVAY NEVCKLVRLP
EAPAAPPQQL PPAALRGVEE RVPEGGPPGA RSNGALPGAA ALEAEEMSEV SQVEEGEVDE
EGPALQALQQ ASLGQLQGLP AAFPPQAAAA AAAAVGKPAP ALTAAADPAQ HVAQGPQPAS
PPFQQQQQQP PAAAPSTVRR DPRLAARARA ETSAQRQQQQ QQQEAAAQPL SAEATEAPQP
QPEPQEPQES PCQQPQQQQQ QAKWDPSVLP PQLRRQPLLS GKLPLLLDLD NTLLHAQAVG
VAGYNIALED WLDEDGLPEV YKFELPCNRK VYYLKLRPGL RRFLKALAPV FELSIYTNAT
QEYADLVVAI LDPDRSLFGD RIVARESSGR GEQTENKTVR CLYGDLDRRC VVAFDDRQNI
WTDLPVSHVV KAQHYDFFDS SRPELLAHYP HLPLEETLAA IAENPRQRAT ALDRPSPVPA
AMKHLNRPYD WDRHMQHMIN IFLKVHQEFF KDPWNANVGT IISGFQSRVL AGVGLFLTGY
RKSFAPGSLV ADCEERQAEL AQRLGATVYR RFDEPGVTHV MAGKSNTNNM LALKERSFQH
LKKVHTLWLF ACESMWAKAP ESCFDADALC ALYDNQPPCA PFKDHWMHLA EFVPPPAVAP
AQPLPLQDRL PVREFLGTGP YSDGASLISP FEETIFLWRP EKQPIRQLYS KASTQHSPPT
LAAGSPHPQQ QLQQQLLPLR PEGQNVGQGR EEMTARSGRQ EAEVMPFCNF QVYAV
//
