GenomeNet

Database: UniProt
Entry: X6LVU0_RETFI
LinkDB: X6LVU0_RETFI
Original site: X6LVU0_RETFI 
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}.
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; 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
//
DBGET integrated database retrieval system