ID G3HI87_CRIGR Unreviewed; 246 AA.
AC G3HI87;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=AlkB homolog 2, alpha-ketoglutarate dependent dioxygenase {ECO:0000313|Ensembl:ENSCGRP00001024363.1};
DE SubName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB-like 2 {ECO:0000313|EMBL:EGW10623.1};
DE SubName: Full=DNA oxidative demethylase ALKBH2 {ECO:0000313|RefSeq:XP_027271784.1};
GN Name=Alkbh2 {ECO:0000313|Ensembl:ENSCGRP00001024363.1,
GN ECO:0000313|RefSeq:XP_027271784.1};
GN ORFNames=I79_010354 {ECO:0000313|EMBL:EGW10623.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW10623.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2] {ECO:0000313|EMBL:EGW10623.1}
RP NUCLEOTIDE SEQUENCE.
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSCGRP00001024363.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:XP_027271784.1}
RP IDENTIFICATION.
RC STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027271784.1};
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_027271784.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
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DR EMBL; JH000399; EGW10623.1; -; Genomic_DNA.
DR RefSeq; XP_003503575.2; XM_003503527.3.
DR RefSeq; XP_007607193.1; XM_007609003.2.
DR RefSeq; XP_027271784.1; XM_027415983.2.
DR STRING; 10029.G3HI87; -.
DR PaxDb; 10029-XP_007607193-1; -.
DR Ensembl; ENSCGRT00001028609.1; ENSCGRP00001024363.1; ENSCGRG00001022310.1.
DR GeneID; 100753724; -.
DR KEGG; cge:100753724; -.
DR CTD; 121642; -.
DR eggNOG; ENOG502QTDK; Eukaryota.
DR GeneTree; ENSGT00940000159009; -.
DR OMA; TQHHWQH; -.
DR OrthoDB; 5483680at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR Proteomes; UP000694386; Unplaced.
DR Proteomes; UP001108280; Chromosome 4.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0051747; F:cytosine C-5 DNA demethylase activity; IEA:Ensembl.
DR GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; IEA:Ensembl.
DR GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl.
DR GO; GO:0035516; F:oxidative DNA demethylase activity; IEA:Ensembl.
DR GO; GO:0000182; F:rDNA binding; IEA:Ensembl.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:Ensembl.
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 Dioxygenase {ECO:0000313|EMBL:EGW10623.1};
KW Oxidoreductase {ECO:0000313|EMBL:EGW10623.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075}.
FT DOMAIN 137..242
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 107..109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 144
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 146
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 156
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 221
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 233
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 237
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT BINDING 239
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ SEQUENCE 246 AA; 27520 MW; 45CF9FE48455E0CA CRC64;
MAVQGGGMDR FLVKPDPGDL GAGGEESAPS GGASGGQPSP NWRHLRAQGL NCDYTVLFGK
AEADEIFREL EQEVEYFTGA LAKVQVFGKW HSVPRKQATY GDAGLTYTFS GLTLTPKPWI
PVLERVRDRV CRVTGQSFNF VLINRYKDGC DHIGEHRDDE RELAPGSPIA SVSFGACRDF
LFRHKDSRGK RPRQTVEVVR LQLAHGSLLM MNHPTNAHWY HSLPIRKKVL APRVNLTFRK
ILHTKK
//