ID E5R0T5_ARTGP Unreviewed; 260 AA.
AC E5R0T5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN ORFNames=MGYG_00630 {ECO:0000313|EMBL:EFQ97591.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; DS989822; EFQ97591.1; -; Genomic_DNA.
DR RefSeq; XP_003176543.1; XM_003176495.1.
DR AlphaFoldDB; E5R0T5; -.
DR GeneID; 10031862; -.
DR VEuPathDB; FungiDB:MGYG_00630; -.
DR eggNOG; ENOG502QR14; Eukaryota.
DR HOGENOM; CLU_041456_0_0_1; -.
DR InParanoid; E5R0T5; -.
DR OMA; VTGGEKW; -.
DR OrthoDB; 5473532at2759; -.
DR Proteomes; UP000002669; 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: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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669}.
FT DOMAIN 52..257
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 260 AA; 28911 MW; BB6E1931223A2439 CRC64;
MPKKAAKETV KVTSKVAAKS KEESPAQKTP NWPALRPLPP TSDLCLTPIL PAQIYIIRNL
FSSALCKTYV SFLASLPLIT TPGRPKKNEA LRVNDRFQVE DASFAELLWS GTGLKELICS
TSSAGQSEDE KVDWDGEVLG LNPNIRVYRY TKGQFFGQHY DESVQVMHGT PPVKGRTSWT
LLIYLSTCSG GETAFYPEPE PELGSRKGKA QQRQPEPVVV GMETGMALLH RHGDECLLHE
GREVMEGEKW VIRSDLVVKR
//
