ID A0A3B4CC12_PYGNA Unreviewed; 360 AA.
AC A0A3B4CC12;
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 Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000009487.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000009487.1}
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}.
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DR RefSeq; XP_017572756.1; XM_017717267.1.
DR AlphaFoldDB; A0A3B4CC12; -.
DR SMR; A0A3B4CC12; -.
DR STRING; 42514.ENSPNAP00000009487; -.
DR Ensembl; ENSPNAT00000015850.1; ENSPNAP00000009487.1; ENSPNAG00000014968.1.
DR GeneID; 108439073; -.
DR CTD; 54890; -.
DR GeneTree; ENSGT00390000009298; -.
DR OMA; ENYWRRD; -.
DR OrthoDB; 179931at2759; -.
DR Proteomes; UP000261440; 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 128..247
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB-like"
FT /evidence="ECO:0000259|Pfam:PF13532"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 41393 MW; C6C864CA49F45F3F CRC64;
MKMSAGGFTD LREKLKAMTP HREEQRSGGE KRRRRSPSDE DEEEEEEVVT RELEARKVKR
GIAQARVFTP EECTHIEAKI DEVVARGERG LYREHTVDRA PLRNKYFFGE GYTYGPRLER
RGPGQERLYS KGEVDEIPSW VHELVISRLV ARGLIPEGFV DSAVINDYQP GGCIVSHVDP
IHIFERPIVS VSFFSDSALC FGCKFQFRPI RVSEPVLCVP VRRGSVTVLS GYAADDITHC
IRPQDIKERR AVIILRKTRP NAPRLDTNPL SPSITLPSER RHKLKAKRSH RKADPDAAHR
PRILEMDKEQ QRLSLFSRQD RRGSADSENS WRRVDAASLY KHSHHTHTDA PSRQVKMRRH
//
