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Database: UniProt
Entry: A0A1V9ZC24_9STRA
LinkDB: A0A1V9ZC24_9STRA
Original site: A0A1V9ZC24_9STRA 
ID   A0A1V9ZC24_9STRA        Unreviewed;      1103 AA.
AC   A0A1V9ZC24;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Protein-serine/threonine phosphatase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=THRCLA_07784 {ECO:0000313|EMBL:OQR95534.1};
OS   Thraustotheca clavata.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Thraustotheca.
OX   NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR95534.1, ECO:0000313|Proteomes:UP000243217};
RN   [1] {ECO:0000313|EMBL:OQR95534.1, ECO:0000313|Proteomes:UP000243217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR95534.1,
RC   ECO:0000313|Proteomes:UP000243217};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
CC   -!- SIMILARITY: Belongs to the NPR2 family.
CC       {ECO:0000256|ARBA:ARBA00008433}.
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:OQR95534.1}.
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DR   EMBL; JNBS01002090; OQR95534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9ZC24; -.
DR   STRING; 74557.A0A1V9ZC24; -.
DR   OrthoDB; 46494at2759; -.
DR   Proteomes; UP000243217; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:UniProt.
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   Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR011947; FCP1_euk.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR009348; NPR2-like.
DR   NCBIfam; TIGR02250; FCP1_euk; 1.
DR   PANTHER; PTHR12991:SF10; GATOR COMPLEX PROTEIN NPRL2; 1.
DR   PANTHER; PTHR12991; NITROGEN PERMEASE REGULATOR 2/TUMOR SUPPRESSOR CANDIDATE 4; 1.
DR   Pfam; PF03031; NIF; 1.
DR   Pfam; PF06218; NPR2; 1.
DR   SMART; SM00292; BRCT; 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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000243217}.
FT   DOMAIN          568..735
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
FT   DOMAIN          772..868
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          373..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          905..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1046..1079
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1046..1073
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1103 AA;  124585 MW;  4F396085511AA616 CRC64;
     MIQAIFYSEF DNIAGPQIVY QAPPNALSNE VFDSVSGYII IDKALCGKII TVCPQDIKIV
     GYPVCIEDDK YHRNALLFNI GFVFHRTMDS TPYKPILRKL GSLMETMEKE SGFLSQESTK
     SKLATILPAI LNDLTHFGEC TIPIDTANII NLKLFPKLLA PPNVHDYEVP VAIRDLKTLL
     QNSAEWDLAL QKIVPFIDGV NYVKRIAITA EVDLSIVKNC MRQLLYYGCI TMIDIFLHTN
     IYTTTEKISM LMNDADLQRA CVNYVAKDED NPPTFQTVFN FYCAFQPGIT VSQIWNSKTG
     QQQQQQQPTQ QLQPQALLVD LRRLVTFGLI HGFLRRIHRY PIAIDRSQRA APPLSSSPSS
     VNVAGLTAPN PSALVRVKTS PPQGVRDKDK VKKMMDGEHH TDEICCAFML RFSDLENILQ
     SEPHLGTQLN FAWTKHLIDV MAAQVVTLSC KGDVQVDWKC SSGQLVYLDQ IVASYGTLAM
     KNEGKLVAPA TGIITILPLS TTESNEKEIQ VATIELCMHP IVQNHRCVVC MRKVEQETVK
     VILPQGRIME VNQAVAKELD GENIERMLKH KKLMLVLDLD HTLLHAVRTT DLVGEVDDEA
     MRFYIPNIPT EHVLKLRPGL STFLSELSTL YDLHIYTHGT RSYAERITEI IDPDNTLFRH
     RIVARTDTPD VGHKSLKLLF PSCDDSMIVV LDDRVDVWKE NSDNVFIIEA FHYFNTRAEI
     NNASGGQVKA EVKERKPDNH LTKALRILKL VHEKFYQTTN GQLNVKYIME NMRHNVLRGC
     NIVFSGVIPI DIPPENDYIW KLATSFGAKP SMTMENFPIT HLVIHPKRLG TKKYLEALKM
     PNVNVVNPQW LIDCASEWMR LREDRYRIRT FAQTPKTEEE KEAGIEETKE SEIVDVTENA
     QEVPKVDDVN EEETKEDSSI PPVFSSTRPP PAKGILVKQA KAKDGNKGVA FDKLPEKINA
     PFTTAMRRKP LAMTHIPVPA APVRPKVVAK GVVATGGSFD FLSKMAKRAP APIVKSAPTQ
     PIVPTHRIIP EPEPDIDDIF ARLEREEQNK SKKKEGENMK KNLKRKIDEP SAQARKCGKQ
     TSSGICKIHK CFNSWFCRFT KRR
//
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