ID   A0A1B8B9J4_FUSPO        Unreviewed;       277 AA.
AC   A0A1B8B9J4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN   ORFNames=FPOA_03331 {ECO:0000313|EMBL:OBS29395.1};
OS   Fusarium poae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS29395.1, ECO:0000313|Proteomes:UP000091967};
RN   [1] {ECO:0000313|EMBL:OBS29395.1, ECO:0000313|Proteomes:UP000091967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516 {ECO:0000313|EMBL:OBS29395.1,
RC   ECO:0000313|Proteomes:UP000091967};
RA   Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA   Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT   "Living apart together: crosstalk between the core and supernumerary
RT   genomes in a fungal plant pathogen.";
RL   Submitted (JUN-2016) 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:OBS29395.1}.
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DR   EMBL; LYXU01000001; OBS29395.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8B9J4; -.
DR   STRING; 36050.A0A1B8B9J4; -.
DR   OMA; YEDTRKC; -.
DR   OrthoDB; 5471288at2759; -.
DR   Proteomes; UP000091967; 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.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000091967}.
FT   DOMAIN          45..256
FT                   /note="Prolyl 4-hydroxylase alpha subunit"
FT                   /evidence="ECO:0000259|SMART:SM00702"
SQ   SEQUENCE   277 AA;  31593 MW;  4FCA6FF82D5911C4 CRC64;
     MAQKIEYKSN EIPIPDSFLA SPSPTPITSH QIDFANSPLP QYDGHTALVL NNVLSPDECR
     ELLSLAEESV PRDDETQSAW KPALVSGGDG YESRAPGYRE SDRIIWDQQT IVDRLWERCL
     QADGLRDLLA VVPHEPWMKG GQFVFSRLND RMRFLKYSPG QYFKPHCDGA YFYTEGPGKE
     FETFYTVHLY LNDSVENDPT AELQGGATSF LDRKGEKRVD VNPKAGSVLI FQHKGLFHEG
     ALVNKGIKYT MRTDILYEWI PDNDEEEEPQ TKAAWWE
//