ID A0A1U7Q8J9_MESAU Unreviewed; 395 AA.
AC A0A1U7Q8J9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
GN Name=Alkbh5 {ECO:0000313|RefSeq:XP_005067729.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005067729.1};
RN [1] {ECO:0000313|RefSeq:XP_005067729.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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_005067729.1; XM_005067672.3.
DR AlphaFoldDB; A0A1U7Q8J9; -.
DR SMR; A0A1U7Q8J9; -.
DR STRING; 10036.ENSMAUP00000012778; -.
DR GeneID; 101841527; -.
DR KEGG; maua:101841527; -.
DR CTD; 54890; -.
DR eggNOG; KOG4176; Eukaryota.
DR OrthoDB; 179931at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0042382; C:paraspeckles; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140693; F:molecular condensate scaffold activity; IEA:Ensembl.
DR GO; GO:1990931; F:mRNA N6-methyladenosine dioxygenase activity; IEA:Ensembl.
DR GO; GO:0046630; P:gamma-delta T cell proliferation; IEA:Ensembl.
DR GO; GO:0061157; P:mRNA destabilization; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:Ensembl.
DR GO; GO:0140694; P:non-membrane-bounded organelle assembly; IEA:Ensembl.
DR GO; GO:0035553; P:oxidative single-stranded RNA demethylation; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706}.
FT DOMAIN 115..275
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB-like"
FT /evidence="ECO:0000259|Pfam:PF13532"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 44397 MW; 2A545390F81273A7 CRC64;
MAAAGGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP YPVSGTTKRK
YQEDSDPERS DYEEQQLQKE EEARKVKSGI RQIRLFSQDE CSKIEARIDE VVSRAEKGLY
NEHTVDRAPL RNKYFFGEGY TYGAQLQKRG PGQERLYPPG DVDEIPEWVH QLVIQKLVEH
RVIPEGFVNS AVINDYQPGG CIVSHVDPIH IFERPIVSVS FFSDSALCFG CKFQFKPIRV
SEPVLSLPVR RGSVTVLSGY AADEITHCIR PQDIKERRAV IILRKTRLDA PRLETKSLSS
STLPPNYASD RLSGNSRDPV LKPKRSHRKA DPDAAHRPRI LEMDKEENRR SVLLPTHRRR
GSFSSENYWR KSYESSDDCP EGAGSPTRKV KMRRH
//
