ID A0A2N5UDQ4_9BASI Unreviewed; 513 AA.
AC A0A2N5UDQ4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN ORFNames=PCANC_22923 {ECO:0000313|EMBL:PLW35865.1}, PCASD_26381
GN {ECO:0000313|EMBL:PLW05084.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW35865.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW35865.1}, and 12SD80
RC {ECO:0000313|EMBL:PLW05084.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) 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 -!- 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:PLW35865.1}.
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DR EMBL; PGCI01001404; PLW05084.1; -; Genomic_DNA.
DR EMBL; PGCJ01000249; PLW35865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5UDQ4; -.
DR STRING; 200324.A0A2N5UDQ4; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR Proteomes; UP000235392; 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:SF565; AT28366P-RELATED; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
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:UP000235388}.
FT DOMAIN 72..352
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 55570 MW; 88289F46700E8555 CRC64;
MPSIRKNPQD EQNTSDFGAS QLYSSPTKQT NGQQRQHRRR TKTPITPQNM GQTLSEPVIT
KHTGSGEDED FAFGVSEMQG WRLTMEDAHA AVLDLNHAPP NSSTNSSAPT EPSKERTRFF
AVYDGHGGAA VAKFSGDTVH FRLRSTPEYQ SGDYQAALKR AFLATDEDLR SNPEFLNDPS
GCTAVAALIT PDGKILVANA GDSRSVLCVN GVAEPMSHDH KPVNRGENNR IVAAGGFVEF
GRVNGNLALS RAIGDFEFKQ NKNLSPEAQV VTANPDILVH QITAEDEFLI LACDGIWDVY
SNQQVVDRVR RLLGERKTLE QVAEQMIDYC LAPDCEWGGV GCDNMTFMVV AILGGKTKEQ
WYDMISERLE RGEGYQTPST FPQPYARGPR GEMLMNNLNQ GSLTNGEDEA TPPSYQNSEN
PADGGSPPGH NAPSAGSLFS LAPVSIIEAL SRVSNVNSYD PTSQSEQPTS DSSDSTSTDK
PESTTTTDAP DSSTIDSTTL SHSDDPSRPT SDA
//