ID D2V646_NAEGR Unreviewed; 563 AA.
AC D2V646;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=NAEGRDRAFT_78740 {ECO:0000313|EMBL:EFC47767.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC47767.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC47767.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; GG738853; EFC47767.1; -; Genomic_DNA.
DR RefSeq; XP_002680511.1; XM_002680465.1.
DR AlphaFoldDB; D2V646; -.
DR STRING; 5762.D2V646; -.
DR EnsemblProtists; EFC47767; EFC47767; NAEGRDRAFT_78740.
DR GeneID; 8861929; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_78740; -.
DR InParanoid; D2V646; -.
DR OrthoDB; 5479078at2759; -.
DR Proteomes; UP000006671; 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; IPR045054; P4HA-like.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR10869:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000006671}.
FT DOMAIN 112..205
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..386
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 64783 MW; 5BCF6FDB5C6450B7 CRC64;
MPPSKKTKRS SSENKEEAKS RSADLSTDSD EKLQYFSLAE GIVSIPKLLS KADCEEQIRK
SYDYTFEESE VGNSSRKKNV GNKKVRNSEQ VELNDEELSK KVFVKCEDAI KKMVGCLQTL
YKKGQFFNSH IDSGRNIEGH PSFITVLIYL NDDFEGGETV FEDEDVTIEP ELGKCVLFLH
QIKHTAEEIT KNTKFVIKSA VLFEENENYE KQLAEKFFSG ESNKTKLEGS VIVQVGDEAF
NMSVENIGNF TDSMLYTLIN TEMASDVEIN KDGIRVFKFP SQDPHIFKRF ILPIFNQADH
LDFPFNFDPS EEEKIDSEFK YWGLLSPFDK NSISNEIKYS NKQEPWKSAE LSLISKPLEF
NLEKQKNELE AKLAILKAIK EVKEKLKFDF SYKKKYKSTF EMISAVKENL ENKYEVIILN
HFYDENFFLL GSDKELFETC LALFGGPEFV SVSNLKFVME SRDSEQNASS VIISDQSDIT
SKSKYDFEMH NMASNLIDEK NIKDPNELEE ELDLCGLKVK GIDLTTKASK EKSWEGEYND
EYYPSYSLFK LTGILINVKR LQE
//
