ID G4UIX0_NEUT9 Unreviewed; 494 AA.
AC G4UIX0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=NEUTE2DRAFT_165345 {ECO:0000313|EMBL:EGZ73194.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ73194.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ73194.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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DR EMBL; GL891217; EGZ73194.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UIX0; -.
DR STRING; 510952.G4UIX0; -.
DR eggNOG; ENOG502QUQ4; Eukaryota.
DR HOGENOM; CLU_026011_0_0_1; -.
DR OMA; IDPHPLA; -.
DR Proteomes; UP000008513; 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; PF02845; CUE; 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:UP000008513};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 52..96
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 278..402
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 413..458
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 111..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 54793 MW; 79F3F75EE2B55CE1 CRC64;
MDGSVAMDGF ITRGKRKAES TLEENVDTTQ VKQTITALYN PIDNTPDGDG ESTDIKLAIL
ASLHPDFGPD ALLDLLIAHD GSVEATTEAL KSTQGARQIA KKKPSGITSQ ASLRSFAVPS
TTGDGDHGGA STIPKKPKLL SRKGATLHLY DPSDISTHTP CTVIHNFLPP SVANSLLVEL
LEEAKTFGKA TFKLFDNVVS SPHTSGFFVG SDYELAEQKS AYFYNGARLS DIRRLTPQLE
TVRPLVQDAV NHEIQQRIRT HHLYGGKKLR YQSPDRWSPN AAFVNLYDGP EQNVGWHSDQ
LTYLGPRAVI GSLSLGVARE FRVRRILPKD KDQDGNSSTT SNANLDSLNQ GQISIHLPHN
SLLVMHADMQ EEWKHCVTPA QAIDPHPIAG KRRINVTYRD YRPEFHPRYT PRCACGIPTI
LRVVQKKREN WGRYFWMCHA GNQPGKEACS FFQWAEFDDD GRPLWKKGTG TRTAGLELDT
RESAQAPQSP DMEQ
//
