ID A0A317W9E5_ASPEC Unreviewed; 485 AA.
AC A0A317W9E5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Prolyl 4-hydroxylase {ECO:0000313|EMBL:PWY82759.1};
GN ORFNames=BO83DRAFT_353759 {ECO:0000313|EMBL:PWY82759.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY82759.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY82759.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY82759.1,
RC ECO:0000313|Proteomes:UP000246171};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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:PWY82759.1}.
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DR EMBL; MSFU01000003; PWY82759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317W9E5; -.
DR VEuPathDB; FungiDB:BO83DRAFT_353759; -.
DR OrthoDB; 38879at2759; -.
DR Proteomes; UP000246171; 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 GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
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 PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 356..478
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 53461 MW; 586E0314DF7E5CA9 CRC64;
MAKSKAAKRK RNTQADLPQK VPKAASTVLT PPPDGASREP KNLSTVVPDE DLEITVETLT
TLTQYPSLTK SKACKDLRVA VYEFRQACTT GVNNAEGANL TARITGALAD KRYLEAKILL
AEMRIRGEQP KIGALCRWVR DLDVVSGLST QPEAREKASL ERTPQDLELL GVLDAILRVS
TPIDLRSNAV DSTDPIAFQS IWDLRPNTTP LQVYASVLDK SILNEAPKDP AAIRIIETTP
GPLRKPPNHH PAILYTTLPN AVPLDPVSPS ITYHPHPAVP GLGLALNVLT PSECKAIIAA
GESVNFLPDV PMREDGDMSI LAHNFYWVID TTFHDMLWAR ISKYVPQSIN GRLVRGINRR
FRVYRYVPGA EYRCHIDGAW PPSGILPDDT YVYDASPEDK KQSSMYTFLL YLNDEFEGGE
TTFFMPAARE GTLNAYPVRP VMGAVAIFPH GEANGALLHE GTGVRKGAKY IIRTDVEYDV
KPSEE
//
