ID A0A0D9MRA4_ASPFA Unreviewed; 335 AA.
AC A0A0D9MRA4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=DNA repair family protein {ECO:0000313|EMBL:KJJ30420.1};
GN ORFNames=AFLA70_86g002890 {ECO:0000313|EMBL:KJJ30420.1};
OS Aspergillus flavus (strain ATCC MYA-384 / AF70).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392242 {ECO:0000313|EMBL:KJJ30420.1, ECO:0000313|Proteomes:UP000032444};
RN [1] {ECO:0000313|Proteomes:UP000032444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-384 / AF70 {ECO:0000313|Proteomes:UP000032444};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus flavus AF70.";
RL Submitted (FEB-2015) 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:KJJ30420.1}.
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DR EMBL; JZDT01000760; KJJ30420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D9MRA4; -.
DR OrthoDB; 36492at2759; -.
DR Proteomes; UP000032444; Unassembled WGS sequence.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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; IPR032852; ALKBH2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR31573; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 2; 1.
DR PANTHER; PTHR31573:SF1; DNA OXIDATIVE DEMETHYLASE ALKBH2; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
FT DOMAIN 200..300
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 207
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 209
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 219
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 279
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 291
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 295
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 297
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ SEQUENCE 335 AA; 37762 MW; F7A56EF6674603A0 CRC64;
MSKRIQSFFQ PIPKKPKVGT SSPDPSQPSD PLDIQQQHEQ NQEEQQPPPT NHQTYPFPIP
DLPPDLSKSL TTISTTLKAP KPITNHPHLD LLYFQPLLPP QTANALFHFL RNSLPFYKVQ
YTIHRGKTPT KITTPRFTTV FGVDATSIFT TDQEKTLHDA KTNTPIPPRT KYKHTPRPIP
PCLTHLLQTI QTTTNTPPDY YNFILINYYA TNTDSISYHS DDERFLGPNP SIASLSLGAK
RDFLLKHKPG VEAGKPLKFP LASGDMVVMR GETQGNWLHS IPKRAGEGGG RINVTFRRAL
VPGGTENYYR YNVGDGGVWR WDEREGRMVS VDGEK
//