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Database: UniProt
Entry: A0A0L1JDB0_ASPNO
LinkDB: A0A0L1JDB0_ASPNO
Original site: A0A0L1JDB0_ASPNO 
ID   A0A0L1JDB0_ASPNO        Unreviewed;       336 AA.
AC   A0A0L1JDB0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=ANOM_002340 {ECO:0000313|EMBL:KNG89697.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG89697.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG89697.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG89697.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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:KNG89697.1}.
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DR   EMBL; JNOM01000026; KNG89697.1; -; Genomic_DNA.
DR   RefSeq; XP_015410620.1; XM_015547597.1.
DR   AlphaFoldDB; A0A0L1JDB0; -.
DR   STRING; 1509407.A0A0L1JDB0; -.
DR   GeneID; 26804144; -.
DR   OrthoDB; 1651948at2759; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47990:SF62; SEXUAL DIFFERENTIATION PROCESS PROTEIN ISP7; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT   DOMAIN          180..284
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   336 AA;  37969 MW;  44E4EA012D04ABB7 CRC64;
     MTVSRPAEYK DVRTADLSTI QFSNLFDKDE AELKKLLKAC EKDGFFYLDL QSEGSEKFWK
     DLYEIDSITK EWFSQPADVK LKTPTVSLSH GSSETSFKAV GNQSGAVESL KDGFEALKIG
     KFELDGRWAL PSVAQDNLVL FDQFTAACHF ISKLLLDCIS DELGLKGDAR LETYHRDDCR
     SKSTLYFLHY PHGAQDPSQV GQNMHTDIGS LTILYAPQWG LQVFSPNDGA WEYVEPRPGH
     AIVNVGDTLR FLSNKRLRSA LHRVLPLGGI QKEDRYSISY FLRASDSTEF KDSDGDESSA
     KHWYLKKYEM YELPHSIQKE KTTLSGGMAQ ELLASF
//
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