ALKB8_BOVIN
ID ALKB8_BOVIN Reviewed; 664 AA.
AC A1A4L5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alkylated DNA repair protein alkB homolog 8;
DE AltName: Full=Probable alpha-ketoglutarate-dependent dioxygenase ABH8;
DE AltName: Full=S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8;
DE AltName: Full=tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ABH8;
DE EC=2.1.1.229 {ECO:0000250|UniProtKB:Q96BT7};
GN Name=ALKBH8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methylation of 5-carboxymethyl uridine to 5-
CC methylcarboxymethyl uridine at the wobble position of the anticodon
CC loop in tRNA via its methyltransferase domain. Catalyzes the last step
CC in the formation of 5-methylcarboxymethyl uridine at the wobble
CC position of the anticodon loop in target tRNA. Has a preference for
CC tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys). Binds tRNA and
CC catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of
CC 5-methylcarboxymethyl uridine at the wobble position of the anticodon
CC loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-
CC methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly).
CC Required for normal survival after DNA damage. May inhibit apoptosis
CC and promote cell survival and angiogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q96BT7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carboxymethyluridine(34) in tRNA + S-adenosyl-L-methionine =
CC 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:43208, Rhea:RHEA-COMP:10407, Rhea:RHEA-
CC COMP:10408, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74851,
CC ChEBI:CHEBI:74882; EC=2.1.1.229;
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q96BT7};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q96BT7};
CC -!- SUBUNIT: Interacts with TRMT112. {ECO:0000250|UniProtKB:Q96BT7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96BT7}. Nucleus
CC {ECO:0000250|UniProtKB:Q96BT7}. Note=Predominantly cytoplasmic.
CC {ECO:0000250|UniProtKB:Q96BT7}.
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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DR EMBL; BC126687; AAI26688.1; -; mRNA.
DR RefSeq; NP_001073810.2; NM_001080341.2.
DR AlphaFoldDB; A1A4L5; -.
DR SMR; A1A4L5; -.
DR STRING; 9913.ENSBTAP00000014068; -.
DR PaxDb; A1A4L5; -.
DR PRIDE; A1A4L5; -.
DR Ensembl; ENSBTAT00000079911; ENSBTAP00000072553; ENSBTAG00000010642.
DR GeneID; 781788; -.
DR KEGG; bta:781788; -.
DR CTD; 91801; -.
DR VEuPathDB; HostDB:ENSBTAG00000010642; -.
DR VGNC; VGNC:25839; ALKBH8.
DR eggNOG; KOG1331; Eukaryota.
DR eggNOG; KOG4176; Eukaryota.
DR GeneTree; ENSGT00940000158563; -.
DR HOGENOM; CLU_029501_4_0_1; -.
DR InParanoid; A1A4L5; -.
DR OMA; PWKTKDE; -.
DR OrthoDB; 996085at2759; -.
DR TreeFam; TF316056; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000010642; Expressed in biceps femoris and 105 other tissues.
DR ExpressionAtlas; A1A4L5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0106335; F:tRNA (carboxymethyluridine(34)-5-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
DR CDD; cd12431; RRM_ALKBH8; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR015095; AlkB_hom8_N.
DR InterPro; IPR034256; ALKBH8_RRM.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR Pfam; PF09004; DUF1891; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Iron; Metal-binding; Methyltransferase; Multifunctional enzyme;
KW Nucleus; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW Transferase; Zinc.
FT CHAIN 1..664
FT /note="Alkylated DNA repair protein alkB homolog 8"
FT /id="PRO_0000337124"
FT DOMAIN 43..120
FT /note="RRM"
FT DOMAIN 220..337
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 411..664
FT /note="Methyltransferase domain"
FT /evidence="ECO:0000250"
FT BINDING 227..229
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 238
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 292
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 328
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 334
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
SQ SEQUENCE 664 AA; 75193 MW; CFFF49EB9DEADAE9 CRC64;
MDSNHQSNYK LSKTEKKLLR KQIKARHTLL RHEGIETVSY ATQSLIVANG GLGNQVSRNQ
LLPVLEKCGL VDALLMPPNK PYSCVRYKTV EESKTAYDTL NGKEIVDDLG QKIILYLNFV
EKAQWKELGL QALPPGLKVI EEIISSEDEK MLLESVNWTE DTENQNFQKS LKHRRVKHFG
YEFHYENNNV DKDKPLPGGL PDICESILEK WLKEGFIKHK PDQLTINQYE PGHGIPAHID
THSAFEDEII SLSLGSEIVM DFKHPDGMTV PVMLPCRSLL VMTGESRYLW THGITPRKFD
TVQASKGHKS GIITSDVEDL TLNKRGIRTS FTFRKVRQTP CNCSYPLVCD SQMKETPASF
PESDKEALQL EQDYVHRVYE EIARHFSSTR HTPWPHIVEF LKALPSGSLV ADIGCGNGKY
LGINNELYMI GCDHSQNLVD ICRERQYQAF VCDALAVPIR SGSCDACISI AVIHHFATAE
RRVAALQELV RLLRPGGKAL IYVWAMEQEY NKKKSKYLRE NRTSQGMKEE ISNDASVQEL
LVKQLPNVGN QDSAHSVSSI NDFQDGGCNS KNVANSKLPI HTNRTSFHSQ DLLVPWHFKG
NPGKDKRVEP FGPLGSRDPG PVFHRYYHVF CEGELEAACR TLNNISILQS YYDQGNWCVI
LQKV
