GenomeNet

Database: UniProt
Entry: A0A5N6T1E3_ASPPS
LinkDB: A0A5N6T1E3_ASPPS
Original site: A0A5N6T1E3_ASPPS 
ID   A0A5N6T1E3_ASPPS        Unreviewed;       568 AA.
AC   A0A5N6T1E3;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Phosphatase 2C-like domain-containing protein {ECO:0000313|EMBL:KAE8139903.1};
GN   ORFNames=BDV38DRAFT_41915 {ECO:0000313|EMBL:KAE8139903.1};
OS   Aspergillus pseudotamarii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=132259 {ECO:0000313|EMBL:KAE8139903.1, ECO:0000313|Proteomes:UP000325672};
RN   [1] {ECO:0000313|EMBL:KAE8139903.1, ECO:0000313|Proteomes:UP000325672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117625 {ECO:0000313|EMBL:KAE8139903.1,
RC   ECO:0000313|Proteomes:UP000325672};
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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; ML743564; KAE8139903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N6T1E3; -.
DR   OrthoDB; 11028at2759; -.
DR   Proteomes; UP000325672; 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:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325672}.
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          277..315
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..315
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;  60604 MW;  A8EEE162009B6E84 CRC64;
     MFSGSSSPPK DKSNSVPHSG AVDTQSLSVH PEEGGVTHTS KSLPSGGFFT RRTSEDQGPA
     GEKKRRSSTV TKAATFFTNA KNSLSLSSSP RESSSFNYTV RSPQTLQSLG SMDPALSVPQ
     GSLNNSAGDS LPTPRSSFKV GVTEDRNRKC RRTMEDTHAY LYNFLGTPAP LARADGENQL
     GSSLTPVEAS SVVETDNGYF AIFDGHAGTF AAEWCGKKLH LILEDIMKKN PNTPVPELLD
     QTFTSVDQQL EKLPVKNSGC TAVIALLRWE DRIPSSHSAT GSSALAPAAA AAAKGDSTSE
     ADDTPTQATS TGPSILPKLQ EKAIRQRVLY TANVGDARII LCRNGKALRL SYDHKGSDEN
     EGKRIANAGG LILNNRVNGV LAVTRALGDA YLKDLVTGHP YTTETVVQPD SDEFIILACD
     GLWDVCTDQE AVDLVRNVPD AQEASKILVD YALARFSTDN LSCMVIRLDT DRVKEVINKT
     AEPIGVAGDP SMDVEHGVSE ADKIIEGARK SMANTDIADD SEAAEKVKDE ILHKMADGEP
     GPEMSVDDSN DAPTVSHLNK SDANNGNP
//
DBGET integrated database retrieval system