ID A0A0L1J116_ASPNO Unreviewed; 467 AA.
AC A0A0L1J116;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=CUE domain protein {ECO:0000313|EMBL:KNG85133.1};
GN ORFNames=ANOM_007029 {ECO:0000313|EMBL:KNG85133.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG85133.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG85133.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG85133.1,
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 -!- 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:KNG85133.1}.
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DR EMBL; JNOM01000171; KNG85133.1; -; Genomic_DNA.
DR RefSeq; XP_015406056.1; XM_015552285.1.
DR AlphaFoldDB; A0A0L1J116; -.
DR STRING; 1509407.A0A0L1J116; -.
DR GeneID; 26808833; -.
DR OrthoDB; 325143at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR CDD; cd14279; CUE; 1.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032854; ALKBH3.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR010666; Znf_GRF.
DR PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR PANTHER; PTHR31212:SF4; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51999; ZF_GRF; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 32..74
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 249..386
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 397..442
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 52645 MW; 5FF49031F60B6DA5 CRC64;
MDRFITRKRP RPSSPVLQAA SSSESPLPDE DSTDVKLALL VSLFPEIAQE TLLDVLVSCN
GSVEAAASTI PGQAPPTKKR VVPGTPSVQT SLTSLVLQPD AGQDSPIKRK SLTKKGKTLH
LYSPEDVAAY TPCTIIHNFL PAEQANALLI ELLEESKYFS RYKFQLFDRT VESPHSASVY
VSTPEEYRQH TSEYTYGGTY RSNVRQITPH MQAVSAKVQH TVNNEVHHRI KSFYPDGEKL
KYQSPKEWMP NAAFVNCYDG PSESVGYHSD ELTYLGPRAI IGSLSLGVER EFRVRRIVPS
NDDDESSQSE KDTPTPQSEP KQSRVASDVR ADAQGQISIH LPHNSLLVMH AEMQEEWKHA
IAPAQTVSPH PLSGNRRINI TYRWYRDSLH PRNTPRCRCG MHAILRCAQR KRETRGRYMW
MCYGGFAPGK KSCGFFQWAE FDDDGEPVWN KKQSEDNAPI LRNFVDE
//
