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Database: UniProt
Entry: V9DLA4_9EURO
LinkDB: V9DLA4_9EURO
Original site: V9DLA4_9EURO 
ID   V9DLA4_9EURO            Unreviewed;       233 AA.
AC   V9DLA4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=G647_00153 {ECO:0000313|EMBL:ETI27704.1};
OS   Cladophialophora carrionii CBS 160.54.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI27704.1, ECO:0000313|Proteomes:UP000030678};
RN   [1] {ECO:0000313|EMBL:ETI27704.1, ECO:0000313|Proteomes:UP000030678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI27704.1,
RC   ECO:0000313|Proteomes:UP000030678};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the alkB family.
CC       {ECO:0000256|ARBA:ARBA00007879}.
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DR   EMBL; KB822697; ETI27704.1; -; Genomic_DNA.
DR   RefSeq; XP_008721778.1; XM_008723556.1.
DR   AlphaFoldDB; V9DLA4; -.
DR   GeneID; 19978646; -.
DR   VEuPathDB; FungiDB:G647_00153; -.
DR   HOGENOM; CLU_059836_0_0_1; -.
DR   OrthoDB; 169579at2759; -.
DR   Proteomes; UP000030678; 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   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}.
FT   DOMAIN          92..217
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   233 AA;  26281 MW;  4935729B008D7ED0 CRC64;
     MSVSSVNGLP PSCYYLPSFI TPTEEHRLTN EIRKLPESKW TVLTHRRLLS LPSTLTGPAR
     DTLLAAPLPA YLESIVVRLK EEKYFESTPH KAPNHVLINE YKPGEGIMPH EDGPAYSPVT
     ATVSLGSHTV LDIYKKNEHG EREAKPTWRI LQEPRSLLVT TGDMYVSTLH GISELLVDTE
     LNHESVVNWD LVEDKPLYQS GQAQRQTRIS LTFRDVTKVA KLGGALKFMN KRR
//
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