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Database: UniProt
Entry: A0A2K6MNL8_RHIBE
LinkDB: A0A2K6MNL8_RHIBE
Original site: A0A2K6MNL8_RHIBE 
ID   A0A2K6MNL8_RHIBE        Unreviewed;       261 AA.
AC   A0A2K6MNL8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=AlkB homolog 2, alpha-ketoglutarate dependent dioxygenase {ECO:0000313|Ensembl:ENSRBIP00000037380.1};
GN   Name=ALKBH2 {ECO:0000313|Ensembl:ENSRBIP00000037380.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000037380.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000037380.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000037380.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|ARBA:ARBA00001954};
CC   -!- SIMILARITY: Belongs to the alkB family.
CC       {ECO:0000256|ARBA:ARBA00007879}.
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DR   RefSeq; XP_017735215.1; XM_017879726.1.
DR   RefSeq; XP_017735216.1; XM_017879727.1.
DR   RefSeq; XP_017735217.1; XM_017879728.1.
DR   RefSeq; XP_017735218.1; XM_017879729.1.
DR   AlphaFoldDB; A0A2K6MNL8; -.
DR   STRING; 61621.ENSRBIP00000037380; -.
DR   Ensembl; ENSRBIT00000061393.1; ENSRBIP00000037380.1; ENSRBIG00000042275.1.
DR   GeneID; 108534388; -.
DR   CTD; 121642; -.
DR   GeneTree; ENSGT00940000159009; -.
DR   OMA; TQHHWQH; -.
DR   OrthoDB; 5483680at2759; -.
DR   Proteomes; UP000233180; Unplaced.
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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180}.
FT   DOMAIN          152..257
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         102..104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         122..124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         159
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         161
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         171
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         236
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         248
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         252
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
FT   BINDING         254
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR632852-1"
SQ   SEQUENCE   261 AA;  29379 MW;  A22A5EABF21C6D94 CRC64;
     MDRFLVKGVQ GGLLRKREEQ EPTGEEPAVS GGDKESTKKR PRREAPGNGG RSASPSWRHI
     RAEGLDCSYT VLFAKAEADE IFQELEKEVE YFTGALARVQ VFGKWHSVPR KQATYGDAGL
     TYTFSGLTLS PKPWIPVLER IRDRVSGVTG QTFNFVLINR YKDGCDHIGE HRDDERELAP
     GSPIASVSFG ACRDFVFRHK DSRGKSPSQR VAVVRLPLAH GSLLMMNHPT NTHWYHSLPV
     RKKVLAPRVN LTFRKILLTK K
//
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