ID A0A1J1HBK0_PLARL Unreviewed; 1387 AA.
AC A0A1J1HBK0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-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 Name=NIF3 {ECO:0000313|EMBL:CRH00802.1};
GN ORFNames=PRELSG_1114800 {ECO:0000313|EMBL:CRH00802.1};
OS Plasmodium relictum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX NCBI_TaxID=85471 {ECO:0000313|EMBL:CRH00802.1, ECO:0000313|Proteomes:UP000220158};
RN [1] {ECO:0000313|EMBL:CRH00802.1, ECO:0000313|Proteomes:UP000220158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGS1 {ECO:0000313|EMBL:CRH00802.1,
RC ECO:0000313|Proteomes:UP000220158};
RG Pathogen Informatics;
RL Submitted (APR-2015) 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; LN835306; CRH00802.1; -; Genomic_DNA.
DR VEuPathDB; PlasmoDB:PRELSG_1114800; -.
DR OMA; EYTHDAV; -.
DR OrthoDB; 227228at2759; -.
DR Proteomes; UP000220158; Chromosome 11.
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; cd17729; BRCT_CTDP1; 1.
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, ECO:0000313|EMBL:CRH00802.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000220158}.
FT DOMAIN 940..1115
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 1156..1245
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 48..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 163081 MW; 79D3E7EB655EDFA1 CRC64;
MDAKESCKEV EIESVASTFE ANKNINFFGE NNRNMLILNN SNREIRNSDK MNNDISKMND
TNDDKNDNDN INNVNNIDNY NNINSNYNIE NINIRNEVNI INDNANDSNN NNIGNVNNIY
SNVNSNTTNN NSYYEYNESY CGDLDTSNTR EKLFNKHSNK NMNYDNYSKS NQNNFSINKN
FKNLRNKFNL FNKNSIKQNN LKQNMNKENN ENEDSEKEAI TNNNYHDDFY KRDAPFSTYN
NQGQNKINYR NFHENRKLKN NNINNNSCGD NMNNGDNNIN NEGNSNMSIN DNNHSINNNI
GINRNDQINS NNNGNNNNII INTVKKRRIV KYDNFYKNKQ KKSYYKSFND PIKRYNNNSL
NLNEINSIKN DSSNYNNNDK QKYQNYSSKN SSINFNHQNN EGNMRNSFMK ENYNTTKNSN
RNNNNLNYIY NNMNKGNFNN IAFSLNKYFI PFKNNGGKDD KNVNNENIMN KNKLNNKNIN
LNNNDILNNN FNNVNENCNT NSYDDNCKDK NNNYDNINNY NYSNKCDDSI SDNNDNYKNN
VSGIEDLNNN NNNNNTRNNA PSNFNNLNLV TQNFNIEFLK NYKNNLEHGL NGDKINGNEN
YVKYEENNIK DYNNQNYIEC LSEVSEISDE EEKNIDLNNK ESNKITDEQV NKNNNNCKKW
NMHNLHSGVT ASSIDTCFNQ SDNNKSELMN NLYNFCNYNR NINTDEETNH FYHTTNNNSY
YKKNLKIENK KGVRNTFMNN IITNSFNPNL NYSNDFDLTN SPSSSNSSMN NHKHDMDRKK
KKKKFNYMSV NDSVNNIENR NSINNKISNY LNEDQGEIHN QHINRNPNLF ERGFQEKNEN
YLNQNNNELI MENDNSYDSS CSNSSINDNT TSLRKESKNE KRNKLTLNQI RTEDLFINSY
MPYPPEKYNN IYELHEIKIL SPHILKTKFQ KEGKTYHSTL KDGKLILLLD LDNTLLQATS
FAKFNMDLPL ENFVDENGEA QLYKFYLPSY NFFYYLKFRP YVRQFLQILS LYYELSVYTN
ATREYADVVI AILDPDRTLF SDRIVARCSS ADRDENKHFS RIYPNIDSKY VIAFDDRKDV
WSDIPQSHIL KAEHYNFFEL SKYDILSHFK EASTCKKKFL DMDMHLYYMT KVFLKLHKKF
FEKPLEVDVG KLIEEIMSDT LKNVGVYFTG FRKNSKNAQN VLSADCEERQ KEMALELGAK
IYTNYDLPGV THIVAAKNCT DNLIKSKKSD YNHIYKVHTL WLYHCRGTLE NVDSSYFDAD
ELCKIYNNKP PMHPKKDHWF FGNKHLRKQD DMTDCVKIEN LKSRIFLGTG EYTHDAVIFS
PFEQIHIKWI EKEVKLRQNY DTSYNTISND IKNNDKNQIN DDYADDNYSY DDNTEEDNEY
SSTNSKL
//
