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Database: UniProt
Entry: A0A194UPD0_9PEZI
LinkDB: A0A194UPD0_9PEZI
Original site: A0A194UPD0_9PEZI 
ID   A0A194UPD0_9PEZI        Unreviewed;       347 AA.
AC   A0A194UPD0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Alpha-ketoglutarate-dependent dioxygenase abh1 {ECO:0000313|EMBL:KUI53525.1};
GN   ORFNames=VP1G_00952 {ECO:0000313|EMBL:KUI53525.1};
OS   Valsa mali var. pyri (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI53525.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) 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; KN714669; KUI53525.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194UPD0; -.
DR   STRING; 694573.A0A194UPD0; -.
DR   OrthoDB; 47845at2759; -.
DR   Proteomes; UP000078576; 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, ECO:0000313|EMBL:KUI53525.1};
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:UP000078576}.
FT   DOMAIN          217..346
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         237
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         302
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
SQ   SEQUENCE   347 AA;  39281 MW;  3498FB002DB12D6C CRC64;
     MTVDLTTLDA HEQPSDHLRA IWKGYAKTDN ATLLSSDSID DLSVPEKLAE FRKAGSIPAD
     KIRTAFSHLA GDSDPSILQV EEDVDILHHP LIPVPSLIPP SIQKSLLSRL IHRDLSRPHH
     QTNLHLHHDL PYPKKDAVTN EPQSFFTYPP DSDTIFIPKD PSVHKPLSMK QVMERRLHWV
     TLGGQYDWTN RVYPGEEPPS FPEDVAGLLE TLFPETLAQA AIVNFYTPGD TMMMHRDVSE
     ETDKGLVSVS MGCDALFMVA PNDVGKMSEA ERPAEGEKHY LLLRIRSGDV IYMTGESRYA
     WHGVPKVVKG TCPDYLQDWP AEDGNYEEWR GWMANKRINL NVRQMRD
//
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