ID A0A395SQ67_FUSSP Unreviewed; 494 AA.
AC A0A395SQ67;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Prolyl 4-hydroxylase {ECO:0000313|EMBL:RGP74604.1};
GN ORFNames=FSPOR_1181 {ECO:0000313|EMBL:RGP74604.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP74604.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP74604.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP74604.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP74604.1}.
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DR EMBL; PXOF01000020; RGP74604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SQ67; -.
DR STRING; 5514.A0A395SQ67; -.
DR Proteomes; UP000266152; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT DOMAIN 363..484
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 54564 MW; B73E5B0F0EA128D6 CRC64;
MSKTKSKKRK QNAQAQAQSE NPRKLAKTTS PTIPTPPPDG SSATPFEPKN LHTVVSEEEL
EITIDTLTSL AEYPGLIKSK LCKDLRVAVY DFRQACTTGV NNAAGANLTA QVTAALADRK
YTEARILLAE MKIRGEQPKL GALCRWVRDL DVISGLSTVP DQQGLVKRSE REETLIKVID
AVLRVCGHED RNPNAIIQPS SIALQEIWDL RPDTPTEQVY ATVLDGTLVA SAPDSFKNNL
RIIETTPGPE RKPPNHHDAI LYASTPDAVP LSTTPPPTTY TPHPVVDGLS VATHVLYPEE
CKAIIAAGET VNFVPDAPLR EDGDVSILAH NFYWVVDQTF HDTLWSRIRP FVPASMNGRL
ARGVNRRFRV YRYVPGAEYR AHIDGAWPPS GITKDDTYVY DNSPVEKKQS SLFTFLIYLN
QDFEGGETTY FLPAAREGVL NAYPVRPIMG GAAIFPHGEI NATLHEGTGV RKGAKYVIRT
EIEYDIEPSE EVKV
//
