ID A0A167MPY6_CALVF Unreviewed; 333 AA.
AC A0A167MPY6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Protein phosphatase 2C {ECO:0000313|EMBL:KZO96948.1};
DE Flags: Fragment;
GN ORFNames=CALVIDRAFT_480753 {ECO:0000313|EMBL:KZO96948.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO96948.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO96948.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO96948.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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DR EMBL; KV417282; KZO96948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167MPY6; -.
DR STRING; 1330018.A0A167MPY6; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000076738; 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; 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:UP000076738}.
FT DOMAIN 25..300
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 333
FT /evidence="ECO:0000313|EMBL:KZO96948.1"
SQ SEQUENCE 333 AA; 36828 MW; CBD0C3B4AE954AEC CRC64;
MSHSSLTAAT ATDKTTEEGG DERFAYGSSE MQGWRITMED AHATILNLDE EEGTGERPPA
ERTSFFAVYD GHGGASVARY AGRTVHKRLA EQAEYQQHEY RDALKRAFLL TDEALRADST
FKNDPSGCTA IACLVTPENR IWAANAGDSR AILGQAGRVK PLSYDHKPHG AVESARIRAA
GGWVEYGRVN GNLALSRALG DFEYKKNLSL EPEAQIVTSD PEILDHQITE EDEFMVIACD
GIWDCMSSQN VCDYVRRHVA SRLPLGKICE SIVDYCLAPD ADLEKSGVGC DNMTIVIVAI
LHGRTLEEWY DWVAERVETG HGYETPSEFK PLY
//
