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Database: UniProt
Entry: A0A1V9ZRA0_9STRA
LinkDB: A0A1V9ZRA0_9STRA
Original site: A0A1V9ZRA0_9STRA 
ID   A0A1V9ZRA0_9STRA        Unreviewed;       267 AA.
AC   A0A1V9ZRA0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=ACHHYP_03435 {ECO:0000313|EMBL:OQS00509.1};
OS   Achlya hypogyna.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Achlya.
OX   NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQS00509.1, ECO:0000313|Proteomes:UP000243579};
RN   [1] {ECO:0000313|EMBL:OQS00509.1, ECO:0000313|Proteomes:UP000243579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQS00509.1,
RC   ECO:0000313|Proteomes:UP000243579};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
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:OQS00509.1}.
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DR   EMBL; JNBR01000030; OQS00509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9ZRA0; -.
DR   STRING; 1202772.A0A1V9ZRA0; -.
DR   OrthoDB; 1382259at2759; -.
DR   Proteomes; UP000243579; 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; 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   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:UP000243579}.
FT   DOMAIN          131..242
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   267 AA;  29689 MW;  1EB0BD808ECDFCA0 CRC64;
     MLARRVVTRH LARVGARTFS SAPAFDENTL LPLFPQATQE AIQHGLNTQG FCILRDFASS
     AIAQAMRTEA ERLYAEGHMF QSNSVDAEGR SYPKPNVFAS ELNGNEWDLA PTILHYTRSV
     MLQAPAMLNK LFPGLQMSSR AYASKLAVSL GDGASYPKHC DTAGLPDKRK VTMVYYLNPN
     WAPGHGGELR VFAPNGTHVV EPRADTLAVF WSDLVAHDVL PCETPVEDVA ARRYALTLWL
     VTDNPRQIND KNHHLYPLRQ HHFPDAA
//
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