ID A0A395GXM1_9EURO Unreviewed; 451 AA.
AC A0A395GXM1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Protein phosphatase 2C {ECO:0000313|EMBL:RAL00276.1};
GN ORFNames=BO80DRAFT_455824 {ECO:0000313|EMBL:RAL00276.1};
OS Aspergillus ibericus CBS 121593.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL00276.1, ECO:0000313|Proteomes:UP000249402};
RN [1] {ECO:0000313|EMBL:RAL00276.1, ECO:0000313|Proteomes:UP000249402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL00276.1,
RC ECO:0000313|Proteomes:UP000249402};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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DR EMBL; KZ824441; RAL00276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395GXM1; -.
DR STRING; 1448316.A0A395GXM1; -.
DR VEuPathDB; FungiDB:BO80DRAFT_455824; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000249402; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR13832:SF565; AT28366P-RELATED; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000249402}.
FT DOMAIN 23..298
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 390..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 48957 MW; E4AA621AE9503EEC CRC64;
MGQTLSEPVV EKTSAEGQDE CCIYGVSAMQ GWRISMEDAH ASVLDLQAKF ADQNEKPTDP
DKRLAFFGVY DGHGGDKVAL FAGENVHKIV AKQESFAKGD IEQALKDGFL ATDRAILEDP
KYEEEVSGCT AAVSVISKHK IWVANAGDSR SVLGVKGRAK PLSFDHKPQN EGEKARISAA
GGFVDFGRVN GNLALSRAIG DFEFKKSPEL SPEQQIVTAY PDVTVHDLSD DDEFLVIACD
GIWDCQSSQS VVEFVRRGIA AKQDLYRICE NMMDNCLASN SETGGVGCDN MTMIIIGLLN
GRTKEEWYNQ IAERVANGDG PCAPPEYAEF RGPGIRNQFE ENPDDFDMEN DRARGFSVRS
GRIILLGDGT ELIPEQNDDE LFDQAEEDQD LANQVRRDTP DAARNEREGT PGPQSKDTPR
ADATEISESP SATAEGSSGS AAGTPQKPTS S
//
