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Database: UniProt
Entry: A7S591_NEMVE
LinkDB: A7S591_NEMVE
Original site: A7S591_NEMVE 
ID   A7S591_NEMVE            Unreviewed;       249 AA.
AC   A7S591;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=NEMVEDRAFT_v1g105050 {ECO:0000313|EMBL:EDO41203.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO41203.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO41203.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR   EMBL; DS469581; EDO41203.1; -; Genomic_DNA.
DR   RefSeq; XP_001633266.1; XM_001633216.1.
DR   AlphaFoldDB; A7S591; -.
DR   STRING; 45351.A7S591; -.
DR   EnsemblMetazoa; EDO41203; EDO41203; NEMVEDRAFT_v1g105050.
DR   eggNOG; ENOG502QR2P; Eukaryota.
DR   HOGENOM; CLU_042482_0_0_1; -.
DR   InParanoid; A7S591; -.
DR   OMA; YESFHYT; -.
DR   PhylomeDB; A7S591; -.
DR   Proteomes; UP000001593; 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; IPR039210; OGFOD3.
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; PTHR14650:SF1; 2-OXOGLUTARATE AND IRON-DEPENDENT OXYGENASE DOMAIN-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR14650; PROLYL HYDROXYLASE-RELATED; 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:UP000001593}.
FT   DOMAIN          138..237
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   249 AA;  28051 MW;  2F8F911D7A18D2E3 CRC64;
     MITFVSVDDS VSRKFLNVKC SNDYGTKFKS CVPKKCGRAV MDDVVSFEEA VYLADLAKRG
     MKHGGSSGGP TILDLHSGAL TYGEKFVNIY TLAKKLKTGE LFTKKDFEVY KQVKNKIKNA
     IATEFNIDQN SLYLTKPTFF SRMTAKPAKT IHDEYWHPHI DKTTYGSFYY TSLLYLSDYG
     RNFTGGRFVF VDKNTNHTVE PKTARVSFFT SGSENLHHVE KVKNGTRFAI TVSFTCDPKF
     AITDPSAEP
//
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