ID X6LVU0_RETFI Unreviewed; 501 AA.
AC X6LVU0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE SubName: Full=2OG-Fe(II) oxygenase family protein {ECO:0000313|EMBL:ETO05471.1};
GN ORFNames=RFI_31926 {ECO:0000313|EMBL:ETO05471.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO05471.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO05471.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
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:ETO05471.1}.
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DR EMBL; ASPP01028083; ETO05471.1; -; Genomic_DNA.
DR AlphaFoldDB; X6LVU0; -.
DR EnsemblProtists; ETO05471; ETO05471; RFI_31926.
DR OrthoDB; 5358684at2759; -.
DR Proteomes; UP000023152; 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; PROLYL HYDROXYLASE EGLN3; 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:UP000023152}.
FT DOMAIN 388..501
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 73..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 56845 MW; E315D003E164E1C8 CRC64;
MKKKTQVLPK ASSSFLKKYP WSSFPENVQM SQTKQEELAF ELLPPELKLK ILEKLNLVDG
VLSGTVEAPP LMDFSMPTKI GKSSQQKKKK EQTIDNEENN SKEERVETHS TIITTMHPKT
TEPSPLLFDN IVLNALQENK STTDSNLCFS LQNAVNLQKH GYVVIDDFID GNSQMIVNCV
KQIESMKQNG VLKKAGLNRR EKHIADVHIS DCGVTKLNGT YHWDAHSKHY VHSTSASCTL
APNSDPELSH LFGSKTLTSL SSSHTTTKPI DWVLSCQHVV FYYGASVGGE ERSVSKDLEP
VTSHWQCVAG IEPLPKITTH SNKKNDEKVQ FENVTDSNSV WRSEDVRSDL HAWMHSDDAN
IAKDLRNVIT QIDKIRVWLN KHVQFGCQDT QVQVSCYPGD GSRYRAHLDE VYVDDSTIQS
IRNSEQISAK KTRRITALLY LNERWNTTEC GGAVRIYLSD GVYRDIEPVA GRLLLFNSQW
LPHEVMPVFH RDRFAITLWM Y
//