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Database: UniProt
Entry: A0A135LCG7_PENPA
LinkDB: A0A135LCG7_PENPA
Original site: A0A135LCG7_PENPA 
ID   A0A135LCG7_PENPA        Unreviewed;       301 AA.
AC   A0A135LCG7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Prolyl 4-hydroxylase, alpha subunit {ECO:0000313|EMBL:KXG46662.1};
GN   ORFNames=PGRI_055180 {ECO:0000313|EMBL:KXG46662.1};
OS   Penicillium patulum (Penicillium griseofulvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG46662.1, ECO:0000313|Proteomes:UP000070168};
RN   [1] {ECO:0000313|EMBL:KXG46662.1, ECO:0000313|Proteomes:UP000070168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG3 {ECO:0000313|EMBL:KXG46662.1,
RC   ECO:0000313|Proteomes:UP000070168};
RX   PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA   Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA   Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT   "Genome sequencing and secondary metabolism of the postharvest pathogen
RT   Penicillium griseofulvum.";
RL   BMC Genomics 17:19-19(2016).
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:KXG46662.1}.
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DR   EMBL; LHQR01000069; KXG46662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135LCG7; -.
DR   STRING; 5078.A0A135LCG7; -.
DR   OMA; YIDCEST; -.
DR   OrthoDB; 325120at2759; -.
DR   Proteomes; UP000070168; 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:SF242; P4HC DOMAIN-CONTAINING PROTEIN; 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:UP000070168}.
FT   DOMAIN          94..287
FT                   /note="Prolyl 4-hydroxylase alpha subunit"
FT                   /evidence="ECO:0000259|SMART:SM00702"
SQ   SEQUENCE   301 AA;  34236 MW;  21C9B5183006D67C CRC64;
     MAVNTIERFH VTIPLSVQFE SNAQGVHVVG VSMPDERISI TGIDDQPSIT QTNFEPDDKV
     WPDGLQDLGL IAANESLACP DFSHIEYFTL HEDPLIIYIP KFVSPDEIAH LLETTKETFT
     PSVVYRQGVS SSDENFRKSE NAWPPRDEVL QCIEQRAIRY QNSQSKLLME QLSLQLYREN
     GFFSYHHDQF DSPPNRLNRY STYNVFLQGD CTGGGTHFPL IPRPTESAWC NYIDCESTQP
     GVIFKPIAGS AVYWVNIREN GLGYRETLHA GMPVTSGTKI GMNIWSWKDT RDVNQETFHV
     Q
//
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