ID A0A066VNN5_TILAU Unreviewed; 802 AA.
AC A0A066VNN5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=K437DRAFT_274939 {ECO:0000313|EMBL:KDN43332.1};
OS Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN43332.1, ECO:0000313|Proteomes:UP000027361};
RN [1] {ECO:0000313|EMBL:KDN43332.1, ECO:0000313|Proteomes:UP000027361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBC 951 {ECO:0000313|EMBL:KDN43332.1,
RC ECO:0000313|Proteomes:UP000027361};
RG DOE Joint Genome Institute;
RA Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT 951.";
RL Submitted (MAY-2014) 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 -!- SIMILARITY: Belongs to the dullard family.
CC {ECO:0000256|ARBA:ARBA00038346}.
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:KDN43332.1}.
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DR EMBL; JMSN01000062; KDN43332.1; -; Genomic_DNA.
DR RefSeq; XP_013242351.1; XM_013386897.1.
DR AlphaFoldDB; A0A066VNN5; -.
DR STRING; 1037660.A0A066VNN5; -.
DR GeneID; 25266592; -.
DR HOGENOM; CLU_350973_0_0_1; -.
DR InParanoid; A0A066VNN5; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000027361; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210:SF70; CTD NUCLEAR ENVELOPE PHOSPHATASE 1; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000027361}.
FT DOMAIN 592..785
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 85800 MW; 4AD602D8C3C9141A CRC64;
MNSISYLDSV LSRSLSTSRK GSGTSSPNKR SAMSSGYNNT CGSGGQQLGD DANPRLCLGR
RASDNLLSDR AAAAARPSHA GFGFTPVNPR LAGEAGKEGS TDKNQSDASL WPQGDEDSSM
ESSVDDAGRS RHHEGGSGSA SGFLRGKGNN KSPHKKSHSD HQERCERERV HLRRAGSTPG
DFSWYSNRRV GSTSTTSSKE NYGWGSLWGL TGWGDNSGCA SGGGSNEAST RSSSGGKRRR
KGGLHPSRTA SSSSGVSVGR ASVHSDVTMM SEMERENIVD FEGGEEEEDQ LHVAAPPSRT
SSDTHEGEKS ITEKDQDGNE AERRHLPNVQ DAADGDRTSS ISNRSTLQED SLPLAFATDL
ATSDAKAQVE SGSLFSLNET RAREAQLRVL QCIPSAPPSY EAAVRGEPSE KGPHATIAGE
RDGPAGSGTG ANRFLKSLFR SLQQAILYIL MLPLRLVRRG RLGTGHKIAV GARTASPGTD
ILPPEPSEEP RRSHTVSRRN NGLCGESSHT GHGGEKAVPG ISTGTGENQI STTPQQLVPK
TQSSSRLLPN PHPVENLLGH DPNAKPPQGH VAPGTTQANL PLPKPHLTSS IIHHSPKTLV
LDLDETLIHS TSRSPNWAVL RGGASVSTGG GLLGMDGLGD LLGLRSTGGR LRPHMVEVVL
EGRSVLYHVY KRPWVDHFLR KVATWYNVVI FTASVQEYAD PVIDWLDQGR GLITGRFFRD
ACTYQNGSYL KDLAIVDSDL SKVCLVDNSP ASYHLNPSNG IPIEGWTHDP KDEALLDLLP
VLDSLRFSSD VRHILGVRLL DS
//
