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Database: UniProt
Entry: A0A3B1KB91_ASTMX
LinkDB: A0A3B1KB91_ASTMX
Original site: A0A3B1KB91_ASTMX 
ID   A0A3B1KB91_ASTMX        Unreviewed;       362 AA.
AC   A0A3B1KB91;
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   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000051693.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000051693.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A3B1KB91; -.
DR   SMR; A0A3B1KB91; -.
DR   STRING; 7994.ENSAMXP00000051693; -.
DR   Ensembl; ENSAMXT00000054005.1; ENSAMXP00000051693.1; ENSAMXG00000037092.1.
DR   GeneTree; ENSGT00390000009298; -.
DR   InParanoid; A0A3B1KB91; -.
DR   OrthoDB; 179931at2759; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000037092; Expressed in testis and 14 other cell types or tissues.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467}.
FT   DOMAIN          129..249
FT                   /note="Alpha-ketoglutarate-dependent dioxygenase AlkB-like"
FT                   /evidence="ECO:0000259|Pfam:PF13532"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..355
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  41664 MW;  83FFEF29646FE037 CRC64;
     MSVSGFTDLR EKLKAMTPHR EEPRSGGEKR RRRPPSDEEE EDEEEARVRE REHESEARKV
     KRGITQARVF TAEECARIEA EIDEVVARAE RGLYREHTVD RAPLRNKYFF GEGYTYGPRL
     ERRGPGQERL YSKGEVDEIP AWVHELVISR LVARGLIPEG FVDSAVINDY QPGGCIVSHV
     DPIHIFERPI VSVSFFSDSA LCFGCKFQFR PIRVSEPVLS VPVRRGSVTV LSGYAADDIT
     HCIRPQDIKE RRAVIILRKT RPNAPRLDTS LLSPSISPPP ERRHKLKAKR SHRKADPDAA
     HRPRVLEMDK EEQRLSLSSR QNRHENSGSE NSWRRMEASS LYKHSHHAHA DTPSRQVKMR
     RH
//
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