ID D4AN14_ARTBC Unreviewed; 307 AA.
AC D4AN14;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=ARB_05618 {ECO:0000313|EMBL:EFE35575.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE35575.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the alkB family.
CC {ECO:0000256|ARBA:ARBA00007879}.
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:EFE35575.1}.
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DR EMBL; ABSU01000003; EFE35575.1; -; Genomic_DNA.
DR RefSeq; XP_003016220.1; XM_003016174.1.
DR AlphaFoldDB; D4AN14; -.
DR STRING; 663331.D4AN14; -.
DR GeneID; 9524210; -.
DR KEGG; abe:ARB_05618; -.
DR eggNOG; KOG3200; Eukaryota.
DR HOGENOM; CLU_059836_0_0_1; -.
DR OMA; CIFAESP; -.
DR OrthoDB; 169579at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
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; IPR032862; ALKBH6.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR46030; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 6; 1.
DR PANTHER; PTHR46030:SF1; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 6; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866}.
FT DOMAIN 87..226
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 307 AA; 34245 MW; E129FE48674F99EA CRC64;
MRNTAEGLLD GPGGLERYKI NQLPDTAYYI PNFISEDEEE MLLSKTWPSA LSKSNALLAS
PLPAWLDSPI ASRFQDLCIF AESPHKSPNH VLINEYQPGQ GIMPHEDGSA YYPIVATVSL
AAPIILDIYD KRPNDLPAPE LPPVEKEAVR NQIAPRFRIL QERRSLLVTT GTLYSDFLHG
IAERTSDEDL GPDTICNWGN LGDSQLFGTG KYERQTRISL TYRDVLKVSK LGNSLRFLIY
HIKGSMIHLS LTFSLPNFSL YHFFVAAAEV PSCTAVRITA EKMVLLIIDP GGAARKLNER
YIMHSAV
//
