ID A0A3B4UT72_SERDU Unreviewed; 360 AA.
AC A0A3B4UT72;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RNA demethylase ALKBH5 {ECO:0000256|ARBA:ARBA00018485};
DE EC=1.14.11.53 {ECO:0000256|ARBA:ARBA00012931};
DE AltName: Full=Alkylated DNA repair protein alkB homolog 5 {ECO:0000256|ARBA:ARBA00030726};
DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5 {ECO:0000256|ARBA:ARBA00033313};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000021831.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000021831.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(6)-methyladenosine in mRNA + O2 = an
CC adenosine in mRNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:49520, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74449; EC=1.14.11.53;
CC Evidence={ECO:0000256|ARBA:ARBA00033605};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
CC -!- SIMILARITY: Belongs to the alkB family.
CC {ECO:0000256|ARBA:ARBA00007879}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B4UT72; -.
DR SMR; A0A3B4UT72; -.
DR STRING; 41447.ENSSDUP00000021831; -.
DR Ensembl; ENSSDUT00000022234.1; ENSSDUP00000021831.1; ENSSDUG00000015880.1.
DR GeneTree; ENSGT00390000009298; -.
DR OMA; ENYWRRD; -.
DR OrthoDB; 179931at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035515; F:oxidative RNA demethylase activity; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0035553; P:oxidative single-stranded RNA demethylation; IEA:InterPro.
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; IPR032860; ALKBH5.
DR PANTHER; PTHR32074; RNA DEMETHYLASE ALKBH5; 1.
DR PANTHER; PTHR32074:SF2; RNA DEMETHYLASE ALKBH5; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 92..255
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB-like"
FT /evidence="ECO:0000259|Pfam:PF13532"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 41190 MW; A1D0E1FD42FE74B4 CRC64;
MAASGYSDLR EKLKSMTPHR DEYKNKYVDG TSNGSGKGRK RKNRESDDDE CEYSDDSAEL
REQEARRVRS SILQKSIFTP EECALIEEKI DEVVANGEAG LYREHTVDRA PLRNKYFFGE
GYTYGAQLEK RGPGQERLYR KGEVDEIPSW VHELVIKRLV SNGVIQEGFV NSAVINDYQP
GGCIVSHVDP LHIFARPIVS VSFFSDSALC FGCRFQFKPI RVSEPVFVLP VRRGSVTVLS
GYAADDITHC IRPQDIKERR AVIILRKTRP DAPRLDSDSP LSSSPAERPT PLKAKRSHRK
ADPDAAHRPR VLEMDKEENR HPSLSRHRRH SGSSENYWRR GQDYDKHRES SGRKVKMRRH
//
