ID A0A2J5I0Y7_9EURO Unreviewed; 637 AA.
AC A0A2J5I0Y7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=CUE domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BDW42DRAFT_184232 {ECO:0000313|EMBL:PLN83459.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN83459.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ559519; PLN83459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J5I0Y7; -.
DR OrthoDB; 325143at2759; -.
DR Proteomes; UP000235023; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 194..237
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 410..555
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 566..611
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 458..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 71509 MW; B3BC9A2823D5F094 CRC64;
MSSHGGSPSP PVSPIDEPSA AQQFLQTEVF ELGAQPGLRS LPPGPERDFL TLTWGPIIYR
TIYTPEADDL LPIFLHALAH EIRKALPRCL PGTAEQHVML VNTYSSRLFS SQKMLQQASE
GAVRNAFHNF KVALTLPSIV LPVRLRVCLV IDSWVLEILA ATLEHAEFKG EAPQYGLCPV
KMVEENFPDL YQESTDVKLA QLVSLFPDLS QDTLLDVLVS SAGSVEATAT IISEQLAAAP
IKKRAVSGPS VQTSLISHIT TLGDQTLEPK RRPTKKGQTL HLFSPHDVAV HTPCTIVHNF
LPPDQANALL LELLDESQHF SRYKFQVFDK TVESPHSASV YVSTPEEHRQ HTSVYTYGGT
YRSNVRQITP HMRSVSAKVQ RTVNDEVQKR IRDVYPDGKK LRFQSPKEWM PNAAFVNCYD
GPAESVGYHS DELTYLGPKA IIGSLSLGVE REFRVRRIVP PDEEDTSNPP PESITDVLTA
GDGENPNRKP RKQEASQTRA DVQGQISIHL PHNSLLVMHA EMQEEWKHAI TPAQTISPHP
LSGNRRINIT YRWYRDSLHP QYTPRCQCGQ HAILRCVQRK RETRGRYMWT CYAGFAPGKQ
TCHFFQWAEF DDNGEPLWER KPIEDDARAL ANFSDAT
//
