ID   A0A1S8BNB5_9PEZI        Unreviewed;       288 AA.
AC   A0A1S8BNB5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Prolyl 4-hydroxylase subunit alpha-3 {ECO:0000313|EMBL:OMP88949.1};
GN   ORFNames=BK809_0005670 {ECO:0000313|EMBL:OMP88949.1};
OS   Diplodia seriata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=420778 {ECO:0000313|EMBL:OMP88949.1, ECO:0000313|Proteomes:UP000190776};
RN   [1] {ECO:0000313|EMBL:OMP88949.1, ECO:0000313|Proteomes:UP000190776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F98.1 {ECO:0000313|EMBL:OMP88949.1,
RC   ECO:0000313|Proteomes:UP000190776};
RA   Robert-Siegwald G., Vallet J., Abou-Mansour E., Xu J., Rey P., Bertsch C.,
RA   Rego C., Larignon P., Fontaine F., Lebrun M.-H.;
RT   "Draft genome sequence of Diplodia seriata F98.1, a fungal species involved
RT   in grapevine trunk diseases.";
RL   Submitted (JAN-2017) 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:OMP88949.1}.
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DR   EMBL; MSZU01000074; OMP88949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8BNB5; -.
DR   STRING; 420778.A0A1S8BNB5; -.
DR   OrthoDB; 325120at2759; -.
DR   Proteomes; UP000190776; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190776};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..266
FT                   /note="Prolyl 4-hydroxylase alpha subunit"
FT                   /evidence="ECO:0000259|SMART:SM00702"
SQ   SEQUENCE   288 AA;  32770 MW;  EDE3BD8747F3C3F8 CRC64;
     MEFSIGSIFK YLFYTVVGYV LVGSPLLRIF LNERPQHPDL AEAFARSDRL VIPDENLVCP
     DHGYNVHVLS RDPLVIYIPG FVSAEEAKHM VAISEDKFKP STVWTGEEER LDPSVRVSEK
     AEIERDEVVQ CIEERARLFQ GWRPFTFIEK LWTQRYVSGG HYSYHFDGPT NIARGGRISS
     FMVYLDGNCT GGGTNFPRLE MPPGRQWCQF LDCDDRESEG ITFKPIAGNA VYWENFRPDG
     SGYEEAWHAG LPVQTGTKVG LNIWSWYQPG YDPKAVADNE QPSDKAEL
//