ID A0A0F4G6X1_9PEZI Unreviewed; 325 AA.
AC A0A0F4G6X1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=DNA repair family protein {ECO:0000313|EMBL:KJX93064.1};
GN ORFNames=TI39_contig4423g00003 {ECO:0000313|EMBL:KJX93064.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX93064.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX93064.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX93064.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-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:KJX93064.1}.
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DR EMBL; LAFY01004382; KJX93064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4G6X1; -.
DR STRING; 1047168.A0A0F4G6X1; -.
DR OrthoDB; 36492at2759; -.
DR Proteomes; UP000033647; Unassembled WGS sequence.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT DOMAIN 185..291
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 COMPBIAS 7..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 194
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 204
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 268
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 282
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 286
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 288
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ SEQUENCE 325 AA; 37065 MW; C5BF8F5A6BF6FCF2 CRC64;
MSKRPRTLDS FFASTPSKKQ KAEPESIATT AKTVKDVDVT ASFSRHQQYP FPLPDLPPKI
RDLINFVPAA DAREINDQPD LDLLYFQPYI PKEIERDLFG FLRSQLFFYR VKYNIKRGPV
ETQVNTPRFT TVFGVDDTSR FDEGNLIDAA SGKPVPHNAY KSKPRPIPEC LDVLRQLTEN
VTGCAFNFVL INFYASGDDS ISYHSDDEKF LGPNPAIASM SLGARRDFLI RHKPTPAEHE
SETKPTKFDL HSGDLILMRG KFQSHWLHSI PKRKGGEADK GRINITFRKA MIKSGTDNYY
RYNVGDGEVY KWSETSRTMV AWKTD
//
