ID A0A4Z0YIV1_9PEZI Unreviewed; 652 AA.
AC A0A4Z0YIV1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN ORFNames=E0Z10_g4531 {ECO:0000313|EMBL:TGJ84249.1};
OS Xylaria hypoxylon.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=37992 {ECO:0000313|EMBL:TGJ84249.1, ECO:0000313|Proteomes:UP000297716};
RN [1] {ECO:0000313|EMBL:TGJ84249.1, ECO:0000313|Proteomes:UP000297716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 108379 {ECO:0000313|EMBL:TGJ84249.1,
RC ECO:0000313|Proteomes:UP000297716};
RA Buettner E., Leonhardt S., Gebauer A.M., Liers C., Hofrichter M.,
RA Kellner H.;
RT "Draft genome sequence of Xylaria hypoxylon DSM 108379, a ubiquitous
RT saprotrophic-parasitic fungi on hardwood.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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:TGJ84249.1}.
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DR EMBL; SKBN01000072; TGJ84249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z0YIV1; -.
DR STRING; 37992.A0A4Z0YIV1; -.
DR Proteomes; UP000297716; 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; 2.
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:SF828; [PYRUVATE DEHYDROGENASE [ACETYL-TRANSFERRING]]-PHOSPHATASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 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:UP000297716}.
FT DOMAIN 193..617
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 47..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 70673 MW; F5090841B3E7303C CRC64;
MSLHRGVSKR WSLKDTYGFI ASFCEAETQA HATANYAACR SLQSSTRRFH HQPPVRCSRS
KDHDQDPATA TATATTSPTK SQSFPHITRR GFHTYFVTHL PSSSLHPDSR APPGPHHNLP
RSEAAPHSTK LGVAPVTPAH LPSTRDLTVV RIPLRSAKHH LGATDSRGSR PYNEDANQAG
TIDIPAFAKR IPISLVRSAM KRSGEGTSAD SPYGDPQIFY FGVFDGHGGT QCSDFLRDEL
HGYIEEAAAE FGLKSSLRIK PGAKTVSSSN RNTSIPSITD GQKGGRRDLD NLDNKGPEEV
QVKADIPQLD KRGAINEVEN SDAVKGNPPT PAETSWDRAL KLQRNLVHEY KSTIGGYFRR
FNPPHFNVSR YADPTPDVPV GVEAVLTYAF LRADLDFVTA QAQKQDPDDP YVSDAAVNTD
EILGRPHHVP PSGHGIGGRT RFKGGSTASV ALISTPTPAP FWHPAASSTL LVGHVGDTRI
LLCETTTGLA KPLTSDHHPS APGESHRLRR FAASFVTDSF GEERIQGLAN SRSFGDMGSK
RLGVSAEPEI ARVDLGPAQY SFLVLISDGV SGTLSDQEIV DVVKEAKTPE QGSKDVVSFA
TEVSSNGDNA TCLVVRLGGW ERRSEGGLGS LGTKEMRDYR RNEALDPRRG RR
//
