ID A0A2N5VTA4_9BASI Unreviewed; 603 AA.
AC A0A2N5VTA4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PCANC_07471 {ECO:0000313|EMBL:PLW53234.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW53234.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW53234.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW53234.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) 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:PLW53234.1}.
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DR EMBL; PGCJ01000065; PLW53234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5VTA4; -.
DR STRING; 200324.A0A2N5VTA4; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin 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 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 SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000235388}.
FT DOMAIN 18..61
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 346..463
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 64..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 66885 MW; FA46D1ACD62566FC CRC64;
MSSARAELDS AGPPGSESLD ASIATLASIF EDHDCEQLQA ALHANHSNLD LAIDYLIRQS
RHEAQPDPVL RYSPRRPRQR SPENLSSNKK RRSNSLQSWL SPAGNQHKTP QTSRASLDDQ
NSSLNKHERS QGPSGSQRSP YPGSQVATLR KPVVSTSSLR PMHEVLGQSS SLQSSSLPPK
PIKRATLPPL FLSTPQQVSK HLPCCSLIYG ILPKPLAWNL YDAMVQDCNG TAEGKKKPWI
QNRWWLADRE VQSPHSTAFF IAKPTAHESL ADNYNESAQY WYAGKPLEED AQPRYFLDEM
DEARSTIEST VNQLLSNDPE ILVRAQRDPQ SNPITRYDQE WHGPWRANVA ASNCYRGSKE
NVGWHADQLT YLGPYPTIAS LSLGTTRQFR LRPVANMHQR DPEPMRTFSI SLPHNSLLVM
HGGCQERYKH CIPPQTSLDV FKNPLEPTDT RIERINITFR FYRPDFQPSR KISTPAASSS
SSSAAAATAA PSHGIITPQP APQVSVTPRC HCGIPAVLRA DQKGKVAASH SRQLRHAAEC
SGQTNAHVDF QFFWHCQAGQ QNAGRGCTFF QILNFDSESR GPCLGDIKKQ TVKSGGELGT
DAV
//
