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Database: UniProt
Entry: A0A163HYI4_DIDRA
LinkDB: A0A163HYI4_DIDRA
Original site: A0A163HYI4_DIDRA 
ID   A0A163HYI4_DIDRA        Unreviewed;      1090 AA.
AC   A0A163HYI4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=PhoD-like phosphatase domain-containing protein {ECO:0000259|Pfam:PF19050};
GN   ORFNames=ST47_g3302 {ECO:0000313|EMBL:KZM25528.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM25528.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM25528.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM25528.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
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:KZM25528.1}.
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DR   EMBL; JYNV01000124; KZM25528.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A163HYI4; -.
DR   STRING; 5454.A0A163HYI4; -.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   CDD; cd07389; MPP_PhoD; 1.
DR   Gene3D; 3.60.21.70; PhoD-like phosphatase; 1.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR018946; PhoD-like_MPP.
DR   InterPro; IPR038607; PhoD-like_sf.
DR   InterPro; IPR043904; PhoD_2-like.
DR   PANTHER; PTHR46689; MEMBRANE PROTEIN, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR46689:SF1; PHOD-LIKE PHOSPHATASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF19050; PhoD_2; 2.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT   DOMAIN          134..388
FT                   /note="PhoD-like phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF19050"
FT   DOMAIN          397..556
FT                   /note="PhoD-like phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF19050"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..1090
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..791
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..913
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..929
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..990
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1013
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1090 AA;  121685 MW;  0EE8CDE87A815C81 CRC64;
     MDLLPPSPQE LDDDSAYVDP IEGQSKTSRT GQTMYVKAVD EIVENEDLSR VEDDTGLFSL
     VRGAGAKPTR IHKKDGEKLG KTREISGVRL HAERGVTFWR FNLEIELGST QTRVAYRINH
     GPAIGFWVPA KGESMNIMFH SCNGFSLSVD SKEFCGPDPM WRDVLNSHQS RPFHVMLGGG
     DQIYNDAAMK QTTLFRQWTE NRNPMDKHHT PFSEDMQNEL EQFYLDRYSM WFSQGLFGMA
     NSQIPMVNIW DDHDIIDGYG SYPHHFMQTP VFTGIGAVAF KYYMLFQHQS VPAETEQTEP
     SWLLGKNPGP YIKERSRSVF MHLGQQLAFL GLDCRTERQR DEILTEDSYD IIFDRLEDEI
     IKGKTKHLIV LLGVPIAYPR LNFLENILTS RLMDPIKAMG RAGMLGGFVN RFDGGVEILD
     DLDDHWTAKH HKEERNWFIK ELQHIAETKS VRVTILGGDV HLGAVGQFYS NKKLKIPKDK
     DARYMPNVIS SAIVNTPPPD MMADVLNKRN KVHHLDANTD EDMIPIFTHD VDGKKRNNNH
     LLPHRNWCSI REYKPGSSPP GTPEPEERPQ PGRRLSDTFN PRQMVRRFSS DQAQRPSARG
     RGPPLSYYNN PQNATADELQ TGVPSQPQSS FSPDRSESER PARSRRNSLT SLFRRRLSVD
     SVGRHESTQS LPPGAHKDPS LERPSNFRRR PSVLTKKGLQ QKPKGDFIDL EGGLDICLNM
     EVSQHDPAGI TMPYRLLVPA LSYAAPEPGV VEKQPRKGSF MGLFGGGRRK KKTIGDDGYS
     QSGSESGSGS DIGEMSEDDE EERAEQRYKV GPRILIPGFG SRNKRASSAN QVHPPDDHLS
     SGFHANEALA SSVHADGSRG VATDRRQSMD TGSTDHGRGA SAWESTAALL PSRSGSLRKT
     PTHNSSHKSQ LPNPESPEFE HDAHVLAHTS SNAKRESYPP HPAIVGAGPG SPYNARGSMQ
     AREDTSGGDY FSSGSRQPRP TSQSRSVSNG HYAPPAPDRA APVLAPVPAP APERTVYPER
     GGYDRTSYPA YPSRNGNAGV GARYLGDGRY EDDDYDSLDD DDRSLSGGEQ AMSQESFVLP
     KPKKKWQIWR
//
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