ID   A0A0D2GY88_9EURO        Unreviewed;       465 AA.
AC   A0A0D2GY88;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   28-JUN-2023, entry version 25.
DE   SubName: Full=Rhinocladiella mackenziei CBS 650.93 unplaced genomic scaffold supercont1.5, whole genome shotgun sequence {ECO:0000313|EMBL:KIX03183.1};
GN   ORFNames=Z518_06735 {ECO:0000313|EMBL:KIX03183.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX03183.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX03183.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX03183.1,
RC   ECO:0000313|Proteomes:UP000053617};
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 Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847479; KIX03183.1; -; Genomic_DNA.
DR   RefSeq; XP_013270319.1; XM_013414865.1.
DR   AlphaFoldDB; A0A0D2GY88; -.
DR   STRING; 1442369.A0A0D2GY88; -.
DR   GeneID; 25294806; -.
DR   VEuPathDB; FungiDB:Z518_06735; -.
DR   HOGENOM; CLU_026011_0_0_1; -.
DR   OrthoDB; 325143at2759; -.
DR   Proteomes; UP000053617; 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   Pfam; PF06839; zf-GRF; 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:UP000053617};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01343}.
FT   DOMAIN          32..76
FT                   /note="CUE"
FT                   /evidence="ECO:0000259|PROSITE:PS51140"
FT   DOMAIN          248..376
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   DOMAIN          387..433
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51999"
FT   REGION          296..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  52474 MW;  F68C3744D40AF616 CRC64;
     MESFISCKRR RVSADTLANP TTPYDEDHEE ETTDVKLAIL SSLYPERHQN DLLEVLLSYE
     GSVNLAIESL SASIKDSPST PTRRLTAPGL QSALPFTLEN KSPSKSGLPP LTRKGKTLHL
     YTPQDIATHT PCSIVHNFLP PDLANALLDE LLAEVPSYES VRFKIFDRVV KSPHTACFYV
     DSLVELQRQR SEYYYNGNDL GDIRQILPVM RQVSDLVRDA VNKEIAIRIR DFYPDSKKLK
     YQSPQEWQPN AAFVNCYDGG AQHVGYHSDQ LSYLGPRPII GSLSLGVARE FRVRKIVPKD
     DPDDNKEKTK SDSSNHPASA ADISGQIAIH LPHNSLLVMH AEMQEEWKHS IAPAVTITPH
     PVAGNKRINI TYRWYREEFR PKHTPKCRCG VPCVLKTVQR QRANRGRYMW MCQVGNKPDG
     GKGCGWFEWA RFTDDGVPVG WKVGGNEDAN RKKREDACDS ELAHD
//