ID A0A1Y1JGP3_PLAGO Unreviewed; 1666 AA.
AC A0A1Y1JGP3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=PGO_111480 {ECO:0000313|EMBL:GAW81699.1};
OS Plasmodium gonderi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=77519 {ECO:0000313|EMBL:GAW81699.1, ECO:0000313|Proteomes:UP000195521};
RN [1] {ECO:0000313|Proteomes:UP000195521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30045 {ECO:0000313|Proteomes:UP000195521};
RA Arisue N., Honma H., Kawai S., Tougan T., Tanabe K., Horii T.;
RT "Plasmodium gonderi genome.";
RL Submitted (APR-2017) 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}.
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:GAW81699.1}.
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DR EMBL; BDQF01000012; GAW81699.1; -; Genomic_DNA.
DR EnsemblProtists; GAW81699; GAW81699; PGO_111480.
DR OMA; CSPLEQI; -.
DR OrthoDB; 227228at2759; -.
DR Proteomes; UP000195521; Unassembled WGS sequence.
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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000195521}.
FT DOMAIN 1194..1370
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 1410..1499
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 27..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1666 AA; 191041 MW; 2BE9B3C83A1E98B2 CRC64;
MEAREGSIDA EVDSIASTLG EHKNKIYYNE GGSSNSGVGD NLRENENSST RNDQMNNENQ
MNEGNNDYDC GVNNIHNYES FNSASYQPNT SAANVVTSSS GVTCTDSNIM IDSVKNQVYN
NINNSCSRNY SADKGTNIYD PTSENKNISA VESTRNFYPY KEGFLDKPEM NNMNGKNFAL
PYSKNVNTSD ANLNNNGSSQ SSSQINSQSN YQSNQYETNK NAKASRNRFN YFNKSEMKNS
MAKQNIRQEN KNNGIDGGGT SVDDNTISYE NEISNEDEQQ RPFSLYNRKN PYGQVNQLNE
YYHRNDENEN ENNETRDMFN TPNEEGFYED YHTRNNQGKN KVHFKNLCEN RKRRKNRKLY
GNLSTDKENK VKGKKHISGN GDSGMEQLEH EVGNNNDDSN NDNNNDSNND NNNDNNNDNN
NDNNNDSNND NNNDNNNDNN NDNNNDNNND NNNDDSFRVS TSVPLEGEKE SDVKIMNSQI
MVKEMPHSNN NIHMNRNDKI IVNVNYNNNG KKRKNVKFDT STFYKHKQKR NYYKFFNDSL
KRYSNNSLKI VNRNVKTNND SSSYANKESE KVHMFLGRNM IKTSSNHLDV DENDKDEVSA
TMNDATVNVV TTNAVTTNAV TTNNAMNATS KDIASDTSDV VAGGVIKPSG RNSNANNLYT
NMKKKSFNNM TFSLNKYLNS YVNFDRIKSK KTNNGNSINK DKIENMCKDA STVGITSVVS
GNSTNVSIGS NNVVSRNNID NTHENWLMNP NQKIYDESLD TYRKGENEFS QSNHTSIGNI
NKFNACTQNL NLELLKNLRN NIQNELNANN NATKESFTVE PNLREMKMHK MKHKCPSYIE
YLSDVSEISD EADSQEEVQV HNDDYLGTDR NSVHKWSNSR IEMKTAASMH GINTVTATSA
ATSGSAASPL GCESNMGLYR NSNSDLMKTS LYNLYNQSKG MDANSNTYGN TNMTDSFSNS
GGNSTVTYSK QMTIRNDLKY YQEVNGISNV FHQDIIKNKD NTYKEDIINY HYKGDMVPSH
FTMNSNMMSY CHPYDINRKT PDAQMDTQYT DYLRMNGKNC FNESNVNIHI KEEMKNKERL
GDKEFQNEIE PSENYLTYRD DTNISAKSDN RGEEKVTSSV KQNRVDMNNE SEEDDKMDEF
SQIGNEDMFI NSYMPYPPEK YNNIYELHEI KILSPHVLKT KFRKEGGNSY HSSLKDGKLI
LLLDLDNTLL QATSFAKFNM ELPLENFLDE NGEPELYKFF LPYYNFFYYL KFRPYVRQFL
QILSLYYELS IYTNATREYA DVVIAILDPD RTLFADRIVA RCSSADREEN KNFSKIYPNV
DAKYVIAFDD RKDVWIDIPH SHILKAEHYN FFELSKYDII SHFKEPTTCK KRFVDMDMHL
HFMTKVFLKL HKQFFERPLE VDVGKLIDNI MLNTLSNVGV YFTGFRKNSK NSQNVLSSDC
EDRQKEIALE LGAKIYSNYD LPGVTHIIAA KNCTDNLIKS KKSNYNHIQK VHTLWLYHCR
GTLQSGNSSY FDADELCKIY NNKPPLHPKK DHWFFGNKDE MRKQDDDSEC VKIENLKSRI
FLGTGEYTND AVICSPLEQI NIKWIEKEVK LRQIYDTVAS STVMPMTDMS PDGGAGYDTT
NDKDTNDEKN PHSDRSPLGE YFDADDNFSY EESNMEEQER EEGKND
//
