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Database: UniProt
Entry: A0A2T4B8T2_9HYPO
LinkDB: A0A2T4B8T2_9HYPO
Original site: A0A2T4B8T2_9HYPO 
ID   A0A2T4B8T2_9HYPO        Unreviewed;       350 AA.
AC   A0A2T4B8T2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=BBK36DRAFT_163551 {ECO:0000313|EMBL:PTB65621.1};
OS   Trichoderma citrinoviride.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB65621.1, ECO:0000313|Proteomes:UP000241546};
RN   [1] {ECO:0000313|Proteomes:UP000241546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG   DOE Joint Genome Institute;
RA   Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA   Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA   Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604574-2};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604574-2};
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DR   EMBL; KZ680214; PTB65621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4B8T2; -.
DR   OrthoDB; 47845at2759; -.
DR   Proteomes; UP000241546; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   InterPro; IPR004574; Alkb.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR16557; ALKYLATED DNA REPAIR PROTEIN ALKB-RELATED; 1.
DR   PANTHER; PTHR16557:SF2; NUCLEIC ACID DIOXYGENASE ALKBH1; 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   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Iron {ECO:0000256|PIRSR:PIRSR604574-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604574-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241546}.
FT   DOMAIN          224..350
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   BINDING         242
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         244
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         304
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
SQ   SEQUENCE   350 AA;  39722 MW;  31A1B06ABC9F6BA5 CRC64;
     MAPGALDLDA HEQPSDQMKA EWKHFARLDQ AALLRGEIPL DDPRRLPLEE TEFRLSGHIP
     REQIAEAFAH LGPEYVDEGR EDGDAPILYH PLLPGLLIIP SLIPPAVQTH LLNTMIHRDL
     SNPTHQTNLH LHYNLPYPSS SSSSPPASFF SLPPTSTTTT PLFTPKDPSV HNPLSIAQVL
     NRRLHWVTLG GQYDWTNRVY PDAAPPQFPA DLAGFLKALF PETLAQAAIV NFYTPGDTMM
     MHRDVSEEVD RGLVSLSFGC DCLFMIAPKE EKEEKKKKKK KYLLLRLRSG DAIYMTQESR
     YAWHGVPKVM KGTCPEYLAD WPAGREDGQY EEWKGWMQNK RINLNVRQMR
//
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