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Database: UniProt
Entry: A0A0D1ZSS8_EXOME
LinkDB: A0A0D1ZSS8_EXOME
Original site: A0A0D1ZSS8_EXOME 
ID   A0A0D1ZSS8_EXOME        Unreviewed;       490 AA.
AC   A0A0D1ZSS8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV10_01341 {ECO:0000313|EMBL:KIV97617.1};
OS   Exophiala mesophila (Black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV97617.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV97617.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV97617.1,
RC   ECO:0000313|Proteomes:UP000054302};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala mesophila CBS40295.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847520; KIV97617.1; -; Genomic_DNA.
DR   RefSeq; XP_016229191.1; XM_016365542.1.
DR   AlphaFoldDB; A0A0D1ZSS8; -.
DR   STRING; 212818.A0A0D1ZSS8; -.
DR   GeneID; 27319186; -.
DR   VEuPathDB; FungiDB:PV10_01341; -.
DR   HOGENOM; CLU_026011_0_0_1; -.
DR   OMA; IDPHPLA; -.
DR   OrthoDB; 325143at2759; -.
DR   Proteomes; UP000054302; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IEA:InterPro.
DR   CDD; cd14279; CUE; 1.
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; IPR032854; ALKBH3.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR010666; Znf_GRF.
DR   PANTHER; PTHR31212; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   PANTHER; PTHR31212:SF4; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 3; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51140; CUE; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS51999; ZF_GRF; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054302};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01343}.
FT   DOMAIN          31..74
FT                   /note="CUE"
FT                   /evidence="ECO:0000259|PROSITE:PS51140"
FT   DOMAIN          263..386
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   DOMAIN          397..443
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  54667 MW;  D03B4D10AACE2FA3 CRC64;
     MDAFLSRKRR RLSPPPAEPL PNEPQEEEED STDVKLAILS SLNPDRSQDD LLEVLLSCDG
     SVSAAIDCLS SSTTTWSSRD IKRRQMIPGI QSAIPFSSTA DPKIKRPSSS SSSSLLSSSK
     QPRQPLTRKG KTLHLYTPDD IATHTPCSII HNFLPSTLAT SLLNELLAES TSYSSISFKI
     FDNVVKSPHT ACFYVDNPID RARQRTEYYY NGNDLLDVRE TLPTTRQVSD LVRIAVNKEI
     ETRIRDFYPD GKKLRFQTEK EWQPNAAFVN CYDGGAQHVG YHSDQLTYLG PRAVIGSLSL
     GVAREFRVRR IVPKDQSSDD ENHPPDAAAA ADLQGQISIH LPHNSLLVMH AEMQEEWKHS
     IAPASTIIPH PVAGNKRINI TYRWYRDEFR PEYTPRCRCD IPCVLKCVQR QRGNRGRYMW
     MCQAGNRPGA GEGCGWFVWA NFTDDGVPVG WKGGGKDNTT SGKTENTGQV VDEGQDNKEG
     HASLPPISIA
//
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