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
//