ID A0A2B7Z3C1_9EURO Unreviewed; 694 AA.
AC A0A2B7Z3C1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=AJ80_00363 {ECO:0000313|EMBL:PGH28105.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH28105.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH28105.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH28105.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004273};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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:PGH28105.1}.
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DR EMBL; PDNA01000002; PGH28105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7Z3C1; -.
DR STRING; 1447883.A0A2B7Z3C1; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000224634; Unassembled WGS sequence.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF484; SERINE_THREONINE-PROTEIN PHOSPHATASE PP-Z1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000224634}.
FT DOMAIN 336..341
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 75420 MW; F1E80447A0EC6CA8 CRC64;
MGQQQSKRSD SSRGSITGTP EKGNGEALQS YPSFSRTDTK DSGRSIRGSI RSKIPGSGKN
DKSDSPRGSS AGLSRIDNGT GDKSDAGSVK SSTSAKSAGS RHNRAGSNAS EQMAVSPSSD
GPAQDLDAPE PPPSPSRSTS LGRGHKSVNA AQKSGEVDHV SDAPPCGTPP TSFFQKPGES
ILIKRDDMVI PVLQELSSAP SVDLNGVNSS PGMGIGALRS IDLDDMITRL LDAGYSTKIT
KGVCLKNAEI VAICTAAREL LLSQPALVEL SAPVKIVGDV HGQYTDLIRL FEMCGFPPAA
NYLFLGDYVD RGKQSLETIL LLLCYKLKYP ENFFLLRGNH ECANVTRVYG FYDECKRRCN
IKIWKTFVDT FNCFPIAAIV AGKIFCVHGG LSPNLSHMDD IRGIARPTDV PDYGLLNDLL
WSDPADMDED WEPNERGVSY CFGKKVIMDF LQRHDFDLVC RAHMVVEDGY EFFNDRVLVT
VFSAPNYCGE FDNWGAIMSV SGELLCSFEL LKPLDSSALK SHIKKGRNKR NSMLNSPPDK
RTGSSPLSPM SFQSFRHRFR RLNYASLSSS QITLPKLSNE SIADELDAFA EAAEAVMELE
APLCPSPSEL RAITLPDHRR RATDAAATIS DESDTVICRR VVVGGGGGGG DSGTELDDRQ
DDIDIETDWE GLPPPLETME ETERCVRQIS LVMD
//
