ID A0A0D2AUI8_9PEZI Unreviewed; 298 AA.
AC A0A0D2AUI8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN ORFNames=PV09_05872 {ECO:0000313|EMBL:KIW02814.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW02814.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW02814.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW02814.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; KN847547; KIW02814.1; -; Genomic_DNA.
DR RefSeq; XP_016212683.1; XM_016359434.1.
DR AlphaFoldDB; A0A0D2AUI8; -.
DR STRING; 253628.A0A0D2AUI8; -.
DR GeneID; 27313845; -.
DR VEuPathDB; FungiDB:PV09_05872; -.
DR HOGENOM; CLU_058132_0_4_1; -.
DR InParanoid; A0A0D2AUI8; -.
DR OrthoDB; 325120at2759; -.
DR Proteomes; UP000053259; 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:UP000053259};
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 74..273
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
SQ SEQUENCE 298 AA; 33797 MW; CAAC938E8D8B621A CRC64;
MAFKPSSLIE YALLAIPLYL FAISPLLRIF FPDVASSTTS SYQSFERTDS LIIPDDTLQC
PPHSYATHIA HHEPLVIYVE NFLSDAEAEH LVALAEKSYQ LSTVFTGEAE SFDPKIRNSS
KALLARDDVV RCIEQRAREF QGWRKDVYIE RLWAQKYEAG GHYTYHYDWS GDLSHRSGGR
LSTFMVYLSA DCEGGGTKFP RLGKPGEGKW CEFVDCEAKD EDGEGEGVVF KPRKGAAVYW
ENFRPDGRGY EETWHAGLPV KSGTKIGLNI WSWWQPGYSE ALNRLETERE AKTSPDEL
//
