ID A0A2J6SIJ6_9HELO Unreviewed; 445 AA.
AC A0A2J6SIJ6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PMD50594.1};
GN ORFNames=K444DRAFT_546987 {ECO:0000313|EMBL:PMD50594.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD50594.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD50594.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD50594.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ613913; PMD50594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6SIJ6; -.
DR STRING; 1095630.A0A2J6SIJ6; -.
DR InParanoid; A0A2J6SIJ6; -.
DR OrthoDB; 325143at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; 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; 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; 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:UP000235371};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 249..367
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 378..423
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 68..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 49871 MW; A02F072AB8A29E1A CRC64;
MDAFVSRKKR KLSSTEPATT IEDISALSSP DDESTDFKLA LLSSLHPYIE QHVLLDILLA
HNGSVEAAST SLKPSDSPPR KPSAATGYQS SLSPFVAQMD SLDGPAKRAK LLSKKGKTLH
LYDPADVAAH TPCTIIHNFL PPEVANALLV ELLKEAPTFE RATFKLFDNV VQSPHTACFY
VESYEEMQRQ KSDYLYNGAL LTDVRQLTPQ MRRVSPIVQE AVNSEITKRV KDHYPNGQKL
KHQSPHSWKP NAANVNCYDG AAESVGYHSD QLTYLGPRAI IGSISLGVAR EFRVRRIVPQ
EEDKKDKSKE DSDAQGQIAI HLPHNSLLVM HAEMQEEWKH SIAPAQAIDP HPISANKRIN
ITYRDYKANL HPRITPRCKC DVPAVLRVVQ RKKENWGKYF WMCHAGNVPG KEGCTFFEWA
KFDDDGEPIF GKQKGKVDET ISREP
//
