ID A0A177DSQ9_ALTAL Unreviewed; 365 AA.
AC A0A177DSQ9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Protein serine/threonine phosphatase 2C {ECO:0000313|EMBL:OAG22557.1};
GN ORFNames=CC77DRAFT_735305 {ECO:0000313|EMBL:OAG22557.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG22557.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG22557.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG22557.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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DR EMBL; KV441474; OAG22557.1; -; Genomic_DNA.
DR RefSeq; XP_018387978.1; XM_018532999.1.
DR AlphaFoldDB; A0A177DSQ9; -.
DR STRING; 5599.A0A177DSQ9; -.
DR GeneID; 29118593; -.
DR KEGG; aalt:CC77DRAFT_735305; -.
DR VEuPathDB; FungiDB:CC77DRAFT_735305; -.
DR OMA; MKGADNC; -.
DR OrthoDB; 45787at2759; -.
DR Proteomes; UP000077248; 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; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 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:UP000077248}.
FT DOMAIN 13..321
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 39484 MW; 9E0265BF3AF58444 CRC64;
MPLVPSSDRD SPLTSSPQIL GARQDQEDRY ITLTPGSIKS RKDLALFAVY DGHGGTATVN
HVAEHLHTHL EHHLSNPKAS NTAEYKHAIQ LALKAVDHEL DRDNLDGGST VSLVLVDTKQ
NLLIQANLGD SHVFFADHEP QSPQSLSPQS PSRVDSGTSS LGWNVEALSV EHAPDSPLEK
RRVEDAGGEI NYRSGIARIG GVSMSRALGD LDYKKPRVNR LAGHDLSDLA GVETGLAPGR
TAIHDLVSNK AHFTVRTLHG QSLILLASDG VGSAKEAEEC TRLAVDGWQS GKEAKQIADE
LTSREGNMKG ADNCTVLVVV LDTESKGRRS IDGGRRSMDI GMEGSGLRRR RRSSIASLKD
WIRDR
//
