ID A0A091DHR8_FUKDA Unreviewed; 238 AA.
AC A0A091DHR8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative alpha-ketoglutarate-dependent dioxygenase ABH6 {ECO:0000313|EMBL:KFO30053.1};
GN ORFNames=H920_08563 {ECO:0000313|EMBL:KFO30053.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO30053.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO30053.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO30053.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the alkB family.
CC {ECO:0000256|ARBA:ARBA00007879}.
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DR EMBL; KN122516; KFO30053.1; -; Genomic_DNA.
DR RefSeq; XP_010630177.1; XM_010631875.1.
DR RefSeq; XP_010630178.1; XM_010631876.1.
DR AlphaFoldDB; A0A091DHR8; -.
DR STRING; 885580.ENSFDAP00000002604; -.
DR Ensembl; ENSFDAT00000028774; ENSFDAP00000002604; ENSFDAG00000012270.
DR GeneID; 104867500; -.
DR CTD; 84964; -.
DR eggNOG; KOG3200; Eukaryota.
DR OMA; ILQDEMY; -.
DR OrthoDB; 169579at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR032862; ALKBH6.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR46030; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 6; 1.
DR PANTHER; PTHR46030:SF1; ALPHA-KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 6; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:KFO30053.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 96..227
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 138..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 238 AA; 26400 MW; EF68BC1E301B0B7F CRC64;
MEEQDARVPA LEPFRVDQAP AVIYYIPDFI SKEEEEYLLR QVFNAPKPKW TQLSGRKLQN
WGGLPHPRGM VLERLPPWLQ RYVDKVSDLS LFGGLPANHV LVNQYLPGEG IMPHEDGPLY
YPTVGTISLG SHTMLDLYKP RQPEDDDATE QPRPPPKPIT SLLLEPCSLL VLRGTAYTHL
LHGIAPAHLD ALDDASLPAN AATCPSAQPG ACLVRGTRVS LTIRRVPRVL RAGLLLSK
//
