ID A9UX55_MONBE Unreviewed; 180 AA.
AC A9UX55;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=MONBRDRAFT_16363 {ECO:0000313|EMBL:EDQ90332.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ90332.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ90332.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
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DR EMBL; CH991548; EDQ90332.1; -; Genomic_DNA.
DR RefSeq; XP_001745099.1; XM_001745047.1.
DR AlphaFoldDB; A9UX55; -.
DR STRING; 81824.A9UX55; -.
DR EnsemblProtists; EDQ90332; EDQ90332; MONBRDRAFT_16363.
DR GeneID; 5890330; -.
DR KEGG; mbr:MONBRDRAFT_16363; -.
DR eggNOG; ENOG502QW9E; Eukaryota.
DR InParanoid; A9UX55; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0051747; F:cytosine C-5 DNA demethylase activity; IBA:GO_Central.
DR GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IBA:GO_Central.
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; IPR032852; ALKBH2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR31573; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 2; 1.
DR PANTHER; PTHR31573:SF1; DNA OXIDATIVE DEMETHYLASE ALKBH2; 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 Reference proteome {ECO:0000313|Proteomes:UP000001357}.
FT DOMAIN 52..160
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 160..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2..4
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 22..24
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 59
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 61
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 71
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 137
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 151
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 155
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 157
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDQ90332.1"
SQ SEQUENCE 180 AA; 20542 MW; 03281752162F7563 CRC64;
VFNKEHVPPR RIAAHGDAGV NYTYSHKTML AAEWTPQLRQ LKEYVEQTTG YEYNFVLINR
YADGRDTIGE HQDNESELDP DVPIASLTLG ATRDFVLRHR DVRRKCGAHS KLNPHTLPLP
SGLLLTMEAP TNKCWYHSVP RRSLARCPGP RINLTFRRIR PGRHPGARPA KRVDRADTKS
//