ID A0A0M0JW27_9EUKA Unreviewed; 558 AA.
AC A0A0M0JW27;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN ORFNames=Ctob_011454 {ECO:0000313|EMBL:KOO30779.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO30779.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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:KOO30779.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JWZX01002166; KOO30779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0JW27; -.
DR OrthoDB; 1382259at2759; -.
DR Proteomes; UP000037460; 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; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 1.
DR PANTHER; PTHR12907:SF26; HIF PROLYL HYDROXYLASE, ISOFORM C; 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:UP000037460}.
FT DOMAIN 208..406
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
FT REGION 29..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 61763 MW; 127BF75F65635F40 CRC64;
MSTHEQLTTR SAKRTVWRRR RCAQLAGALC DSRSPPTKPA PPGAIATTSN SDDELLQAPS
LWLVCNEAGA QLHAGPNAMS TVLGHAPEGD VFEARLLDIA CAWAKLEASE ASRLLGLTAA
YVCTSGAETS IRAFGGRDAW SGELWFEREP LGRVVHAHSP PKHAPPRGSA SSLKRLKAMD
GVKVEAAPPL RALETTLHAD AIASLVDRGY VVVDHALPSA LCRKLRAEML SLEANDQMWN
SRSYGADDEG SAHKHIHETQ LDYKEVRRFA PTFARIEHDP SLIDQLRGCV PGLEQQLGTQ
HVRIQINAGH GGCYTMHTDQ GSVGGSHGQI LHVTALFYLN PDWQSLVYVH AEWQPGDGGE
LRVFPYPRPV EVIAPVEGRL VLFEPRMVHD VLPNYKKRFC FTLWCGVKGA ASSHQIDHET
LSRMELDPSL ASAAAIAEAW RRREQRPLVY DETLPRVMRS LFLPEMRMCL VRMVHGDQEL
RAVTQSHHES AGREDMLYGI RAHHEAISKV NPAWALDLLR QLSAVETTHG EGYITAARGV
VRLAELRDLA HRLGSWWI
//
