ID   A0A423WBY9_9PEZI        Unreviewed;       403 AA.
AC   A0A423WBY9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN   ORFNames=VMCG_06523 {ECO:0000313|EMBL:ROW00780.1};
OS   Valsa malicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW00780.1, ECO:0000313|Proteomes:UP000283895};
RN   [1] {ECO:0000313|EMBL:ROW00780.1, ECO:0000313|Proteomes:UP000283895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-1 {ECO:0000313|EMBL:ROW00780.1,
RC   ECO:0000313|Proteomes:UP000283895};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
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:ROW00780.1}.
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DR   EMBL; LKEA01000020; ROW00780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423WBY9; -.
DR   STRING; 356882.A0A423WBY9; -.
DR   Proteomes; UP000283895; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR045054; P4HA-like.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283895}.
FT   DOMAIN          76..385
FT                   /note="Prolyl 4-hydroxylase alpha subunit"
FT                   /evidence="ECO:0000259|SMART:SM00702"
FT   REGION          104..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..176
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  43245 MW;  702835C34EDAB2E3 CRC64;
     MFDFLRTRKS DDDPRSANAK ALGIPEGEHI HMTYASRDVA LPPDFISLTS PPPDARPVTI
     TPVDWESAGL PGYKGCYAVV LDNVLSPGEC AELIRLAESS VDRARMSPAP SPAPAAAPAP
     AVAPTASSSS SASSSTSSSS SSSPSEDGDD DGDDDGDGDG DGDGDGDGDG DGDGDGDANG
     DGNGGDGGNG NGAWIPAMVN VGGGFEVLDS WYRNSDRIVW DNQEVVDRLW ARCMQGSVGE
     VLRERLAVLD GDESLGCFQR KKPDFKLVKQ RWEFSRVNQR MRFLRYGPGQ FFRPHCDGQY
     GERVDGELYK TFFTLQLYMN DSVAAGGKDA ELVGGATSFL SGDGEQKVDV ECKAGRVLIF
     QHRRLYHAGD DVIKGTKYSM RTDMLYKLVK LEEAETEKPD EGA
//