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Database: UniProt
Entry: A0A022RPM1_ERYGU
LinkDB: A0A022RPM1_ERYGU
Original site: A0A022RPM1_ERYGU 
ID   A0A022RPM1_ERYGU        Unreviewed;       471 AA.
AC   A0A022RPM1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=MIMGU_mgv1a005780mg {ECO:0000313|EMBL:EYU41989.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU41989.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU41989.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604574-2};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604574-2};
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DR   EMBL; KI630319; EYU41989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022RPM1; -.
DR   STRING; 4155.A0A022RPM1; -.
DR   eggNOG; KOG2731; Eukaryota.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR   GO; GO:0035516; F:oxidative DNA demethylase activity; IBA:GO_Central.
DR   GO; GO:0035515; F:oxidative RNA demethylase activity; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0035513; P:oxidative RNA demethylation; IBA:GO_Central.
DR   GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IBA:GO_Central.
DR   GO; GO:0019748; P:secondary metabolic process; IEA:UniProt.
DR   Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR   InterPro; IPR004574; Alkb.
DR   InterPro; IPR027450; AlkB-like.
DR   InterPro; IPR037151; AlkB-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR16557; ALKYLATED DNA REPAIR PROTEIN ALKB-RELATED; 1.
DR   PANTHER; PTHR16557:SF2; NUCLEIC ACID DIOXYGENASE ALKBH1; 1.
DR   Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Iron {ECO:0000256|PIRSR:PIRSR604574-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604574-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT   DOMAIN          361..471
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          24..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         379
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         381
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
FT   BINDING         439
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604574-2"
SQ   SEQUENCE   471 AA;  53207 MW;  31718475DEFC5592 CRC64;
     MQFGLYRTTP LAAAARLSSV LGKMTTNRGM KSSPDARKSL TDNERGQPSI LNMEEFPSLS
     ATKSIPYRKR RNKIDLITTS ERRTEAVVVQ NIGPLHGEAS TSINDSYDTS LPANFGKKTP
     PSFCRKPKPG QNYQEHEVST SINDSYDTSL PADFGKKATP SSFTRKPKPR QNYHEHEASK
     RNSNFSRGTD VDEPFDICFT EPRKSSHRRN SSHDKNSGKW VQKVQSSEEN VHLEDITEKI
     DDVEYSVIER GEVLRPGMVL FKSYIPISEQ RCQEFGRGPG GFYRPGYEDG AKLRLYMMCL
     GLDWNAQSRK YGDIRQHDNV KPPHIPDEFT SLVTKALDDS HTLIKQNFPT ENVEDVLPKM
     SPDVCIVNFY NTNGRLGLHQ DRDESKCSLR KRLPVVSISV GDSAEFLYGD ERDADVADRV
     LLESGDVVIF GGESRHVFHG VKSIIPNSAP RELLENTNLR PGRLNLTFRK Y
//
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