ID A0A0B2X6B8_METAS Unreviewed; 607 AA.
AC A0A0B2X6B8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Protein phosphatase 2C domain containing protein {ECO:0000313|EMBL:KHO01934.1};
GN ORFNames=MAM_00935 {ECO:0000313|EMBL:KHO01934.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHO01934.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHO01934.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHO01934.1,
RC ECO:0000313|Proteomes:UP000030816};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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:KHO01934.1}.
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DR EMBL; AZHE01000001; KHO01934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2X6B8; -.
DR STRING; 1081103.A0A0B2X6B8; -.
DR HOGENOM; CLU_021251_2_0_1; -.
DR OrthoDB; 202023at2759; -.
DR Proteomes; UP000030816; 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; 2.
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:SF828; [PYRUVATE DEHYDROGENASE [ACETYL-TRANSFERRING]]-PHOSPHATASE 2, MITOCHONDRIAL; 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:UP000030816}.
FT DOMAIN 156..572
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 65733 MW; 9E84AEAF6C2BEF74 CRC64;
MPAASPSVLD ARSSASRARR RSRFQPTCAR RRSTCPLVTS RNCVPLPRFP DQLLRHCFHT
YFVTHLPSSS LHPDSHRTIG PGHKLPRDAS TPHTPSSGPS PAAVSIPNMQ SRDLTVVRIP
LRRAKHHFGS ATARGSRPYN EDADQAGTVD IPAFAKRGPL SVRQKPGEPT PADSVLGDPQ
IFYFGVFDGH GGTQCSHFLR DELHGYIEEA ALEFGLQSSL RKSKPGRDQP KPTAGERPIS
NQQALDSVDM KSAEDVQPQM DVPDPENRAF VVDSPNHEPA LPDAKSPPAE SQNMDKAISL
ERDLVKAYRN AVGGYFRRFN PEHFDISSEA GKQASITVES SLAYAFLRAD LDFVSAQARK
ADPDASDQPL NDDEILGAPH TTPSGHGIGG TTRFKGGSTA SVALISTPTT APFWHPAAHS
TLVAAHVGDS RILLCETATG LPHPLTSDHH PTTPTESRRL RRYAPAGSMV TGDSFGEERI
AGLANSRAFG DIRSKRIGVS AEPEITRVEM GPAEFSFLVL MSDGVSGTLS DQEIVDIVKE
ARTPDDGARN IVEYATEVSK DGDNATCQVV RLGGWERRSE GGLGSMGTKE IRDIRKAEAQ
DPRRGKR
//