ID A0A175VW36_9PEZI Unreviewed; 452 AA.
AC A0A175VW36;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB 3 {ECO:0000313|EMBL:KXX75455.1};
GN ORFNames=MMYC01_207586 {ECO:0000313|EMBL:KXX75455.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX75455.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX75455.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXX75455.1}.
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DR EMBL; LCTW02000270; KXX75455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175VW36; -.
DR STRING; 100816.A0A175VW36; -.
DR VEuPathDB; FungiDB:MMYC01_207586; -.
DR OrthoDB; 325143at2759; -.
DR Proteomes; UP000078237; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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 SMART; SM00546; 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 Dioxygenase {ECO:0000313|EMBL:KXX75455.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:KXX75455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078237};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 28..71
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 246..369
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 380..425
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 50617 MW; 019173F9FDDC596C CRC64;
MDAFVTRKKR KSSPEAAAQG QDGPVEESTD IKLAILSSLY PEIDQEALLD ILLAHDGNVD
ATTQALKAPR LSRRSGIGSA VASQSSLRSF AVSSAGLSQS SMSNKRAKLL SRKGATLHLY
DPRDISEHTP CTIIHNFLPA EEANALLVEL LEESKSFEKI TFKLFDNVVS SPHTSGFYVG
SYKELQEQKH EYVYNGSRMT DVRTLTPQLE MVKARVQEAV NREIQERIRT RYGGKKLKYQ
SPSPWSPNAA FVNCYNGPQE SVGWHSDQLT YLGPRPVIGS LSLGVTREFR VRRVLPSSPA
SSLSDDREQQ QYNPDLAGQI AIHLPHNSLL VMHADMQEEW KHSVCPAQAI DPHPLAGNRR
INITYRHYRA GFHPRNTPRC PCGVPAVLRV VTKKHGNWGR YFWMCYAGNV PDKEACEFFR
WADFDDDGNP LGLAQQGQEE RLGGRQEFKG NE
//