ID A0A166D8F3_9AGAM Unreviewed; 213 AA.
AC A0A166D8F3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
DE Flags: Fragment;
GN ORFNames=SISSUDRAFT_957281 {ECO:0000313|EMBL:KZT38248.1};
OS Sistotremastrum suecicum HHB10207 ss-3.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT38248.1, ECO:0000313|Proteomes:UP000076798};
RN [1] {ECO:0000313|EMBL:KZT38248.1, ECO:0000313|Proteomes:UP000076798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT38248.1,
RC ECO:0000313|Proteomes:UP000076798};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; KV428067; KZT38248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166D8F3; -.
DR STRING; 1314776.A0A166D8F3; -.
DR Proteomes; UP000076798; 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.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076798}.
FT DOMAIN 5..212
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZT38248.1"
FT NON_TER 213
FT /evidence="ECO:0000313|EMBL:KZT38248.1"
SQ SEQUENCE 213 AA; 24395 MW; 0939D3D35E552778 CRC64;
EYAKKFALVI DNLFTQADCD KLLAAAGVSL SEENWEVAQI NGGTHEYTDT TYRNSGRKMI
DDHELANWIL EKLRPYLSEI AEIQTFKTHG THRRGPKKAR LLRLNERLRF LRYGRGEFFK
PHCDGAYHTP DGSEVSYYTL QIYINGDEAS LEGGPTRFFA LPDMFSRMSP EKNTLDVPAR
TGRVLIFEQN GMAHSGEEVS RGIKISMRTD FMY
//
