ID A0A0M0J3G7_9EUKA Unreviewed; 473 AA.
AC A0A0M0J3G7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Prolyl 4-hydroxylase alpha subunit domain-containing protein {ECO:0000259|SMART:SM00702};
GN ORFNames=Ctob_002656 {ECO:0000313|EMBL:KOO21060.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO21060.1, 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:KOO21060.1}.
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DR EMBL; JWZX01003392; KOO21060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0J3G7; -.
DR OrthoDB; 5488227at2759; -.
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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10869:SF230; TRANSMEMBRANE PROLYL 4-HYDROXYLASE; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF13414; TPR_11; 1.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 44..77
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 196..386
FT /note="Prolyl 4-hydroxylase alpha subunit"
FT /evidence="ECO:0000259|SMART:SM00702"
FT REGION 392..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 50575 MW; 36F263C6E5D57B93 CRC64;
MAAQQQQQLL MTHYQAAVDA HRSHNLQAAL ASYQEVIAIN PGIAAVHNNV AAIFLSQGKK
LDAEASWRKA IKLKPEYAEA HYNLAIILSE RGDEHLPEAQ QLCEQAIAHK DGYAAAHHLL
GNILSSLQQL DDARTQYQLA EVLAGGGSTP SGGGAPAAAT SAAASFRWEG VEIGHVRTLE
LPDGTRCEME TLALKPLVFR VDHFLTADEC DRIVALARTR LKGSLVMGDA SKAERTSSSV
FLGAAEDALL PELQRRLAAL TNLPLPQVER SEDLQVVHYS TNATFSMHHD SSKFHSRLLT
AFYYLNDVPR GGETAFPAAD KAMTPGEAMK LAEPAAHGLG LIVKPRRGSA LLFYNHDESG
AVDPTAVHAG CRVLEGEKWG ANHWILVNAA PSAPPVAKGS AREATDAEPG AEAAERETES
DGDTPSTGKN AAMNKKKREK AKLKKLHQAP ASVGPSASLS SAWERGEAEG QAD
//
