ID A0A5N6UU95_9EURO Unreviewed; 568 AA.
AC A0A5N6UU95;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 08-NOV-2023, entry version 11.
DE SubName: Full=Phosphatase 2C-like domain-containing protein {ECO:0000313|EMBL:KAE8162070.1};
GN ORFNames=BDV40DRAFT_300703 {ECO:0000313|EMBL:KAE8162070.1};
OS Aspergillus tamarii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41984 {ECO:0000313|EMBL:KAE8162070.1, ECO:0000313|Proteomes:UP000326950};
RN [1] {ECO:0000313|EMBL:KAE8162070.1, ECO:0000313|Proteomes:UP000326950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117626 {ECO:0000313|EMBL:KAE8162070.1,
RC ECO:0000313|Proteomes:UP000326950};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ML738633; KAE8162070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6UU95; -.
DR Proteomes; UP000326950; 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; PROTEIN PHOSPHATASE 2C; 1.
DR PANTHER; PTHR13832:SF837; PROTEIN PHOSPHATASE 2C HOMOLOG 1; 1.
DR Pfam; PF00481; PP2C; 2.
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
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:UP000326950}.
FT DOMAIN 139..468
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 60774 MW; 05E4C3A39877D3C6 CRC64;
MFSGSSSPPK DKSNSVPHSG AVDTQSLSVH PEEGAVTHTS KSLPSGGFFT RRTSEDQGPA
GEKKRRSSTV TKAATFFTNA KNSLSLSSSP RESSSFNYTV RSPQTLQSLG SMDPALSVPQ
GSLNNSAGDS LPTPRSSFKV GVTEDRNRKC RRTMEDTHAY LYNFLGTPAP LARADGENQP
DSSLAPEEAS SVVETDNGYF AIFDGHAGTF AAEWCGKKLH LILEDIMKKN PNTPVPELLD
QTFTSVDQQL EKLPVKNSGC TAVIALLRWE DRIPSSHSAT GSSALAPAAA AAAKGDSNSE
ADDTPTQTTS TGPSILPKLQ EKAIRQRVLY TANVGDARII LCRNGKALRL SYDHKGSDEN
EGKRIANAGG LILNNRVNGV LAVTRALGDA YLKDLVTGHP YTTETVVQPD SDEFIILACD
GLWDVCTDQE AVDLIRNVPD AQEASKILVD YALARFSTDN LSCMVIRLDT NRVKEVINKT
AEPIGVAGDP SMDVEHGVSE ADKIIEGARK SMANADITDD SETAEKVKDE ILHKMADGEP
GPEMSVDDSN DAPTVSHLNK TDANNGKP
//