ID A0A178F2Q3_TRIRU Unreviewed; 695 AA.
AC A0A178F2Q3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=A7C99_1830 {ECO:0000313|EMBL:OAL66444.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL66444.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL66444.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) 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:OAL66444.1}.
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DR EMBL; LHPM01000012; OAL66444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178F2Q3; -.
DR VEuPathDB; FungiDB:TERG_04004; -.
DR Proteomes; UP000243015; 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:SF4; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 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:UP000243015}.
FT DOMAIN 514..668
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT BINDING 532
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 650
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ SEQUENCE 695 AA; 77334 MW; 28324EF951C3D339 CRC64;
MAGTKNGVLK VVGRVGVTRR TRASQRKTLL QANTLLSWAR SGSSSRSSTE KDGIEPQAGQ
ADIVVPALKD ELLEPHGQPP VWAEDRVVLG DALPWFHSVQ GGCYYLDNIC RGVLIDGDCG
DRSYIDDEVV ITRVKTKEGQ LVMTKDHDPN GPILRSLINS MRLEIPVGLI LGGKNADCRT
KVPYNFNVLD FFRITDIWFE QVGKHKGAQM RFEKINLATK SWWSPKGSPD PIPLEQRESV
TPAPDHICLS CSIGTAQVFA QGWMCLNPLC AEFWKMEGSP PPSQLTFAPE FLAKRSKPKN
VVLPPCSLVP DLLSTFSNDQ TDVTGTRMAW KGIVCPQCRA CIARIHWRRW ECSTAGCGFQ
YSPPMNHISL RSVLPDLEMS PSGHKLPTVP KDITSMPTIQ YMKNYRKDTF VLPGAGIVTH
FAANRTVNSC PGGPDDLFSL MQREDLGLRR YPISPCVVAG TLTSHFAVNY GMPYKYIVSV
DSRPFNTAPP VIISALERLK WATRHTVDAN AFQMPNELLA LGYFEDMSIG YHDDGESSLG
PTIATLSLGA PATMLIRMKD EYYNGFRKRD GKDKIYLQHD PVLPGCANEE ARAELARKFN
AKEITAEQYL AARQALPTSR REAPPMCTMA LNHGDLAVMH GPDLQKYYEH SVIPSGRLRF
ALTARYVMPD QVPASEHWKG DYDPIPEFEY DGDET
//