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Database: UniProt
Entry: A0A5N6UU95_9EURO
LinkDB: A0A5N6UU95_9EURO
Original site: A0A5N6UU95_9EURO 
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}.
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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
//
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