ALKB8_XENTR
ID ALKB8_XENTR Reviewed; 628 AA.
AC Q07G10;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 80.
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.-;
DE EC=2.1.1.229 {ECO:0000250|UniProtKB:Q96BT7};
GN Name=alkbh8; ORFNames=TEgg091o15.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA 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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAL49308.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR855607; CAL49308.1; ALT_INIT; mRNA.
DR RefSeq; NP_001017297.2; NM_001017297.3.
DR AlphaFoldDB; Q07G10; -.
DR SMR; Q07G10; -.
DR STRING; 8364.ENSXETP00000031643; -.
DR PaxDb; Q07G10; -.
DR GeneID; 550051; -.
DR KEGG; xtr:550051; -.
DR CTD; 91801; -.
DR Xenbase; XB-GENE-985927; alkbh8.
DR eggNOG; KOG1331; Eukaryota.
DR eggNOG; KOG4176; Eukaryota.
DR InParanoid; Q07G10; -.
DR OrthoDB; 996085at2759; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
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: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: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; 2.60.120.590; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
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; PF08241; Methyltransf_11; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50102; RRM; 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..628
FT /note="Alkylated DNA repair protein alkB homolog 8"
FT /id="PRO_0000337128"
FT DOMAIN 43..123
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 218..335
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 410..628
FT /note="Methyltransferase domain"
FT /evidence="ECO:0000250"
FT REGION 563..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..227
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
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="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 290
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 326
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 332
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q96BT7"
SQ SEQUENCE 628 AA; 70022 MW; 3F4376A29FAF8D6B CRC64;
MGSIDGTRPK LSKDNKKLLK KQAKAKHILL KHEGIETVLH LSQSLVVANG GLGNGVSRQQ
LLAVLERCGK VETLLMPPNK PYAFVTYSSA EEAIKAYSSL SGQELCGEDA EQPITLYLSF
VEKVVVKEVL SPSLPPGLII VEDFVSPEQE RTMLESIDWD SETSSQKSLK HRQVKHYGYE
FRYDNNNVDK DKPLPGGLPD FCTEALRKCV QRGLIKHDPD QLTINQYEPG QGIPPHVDTH
SAFEDEILSL SLGAEIVMDF KHPNGSVVPV MLPQRSLLIM SGESRYLWTH GITPRKFDVI
QVSEGQTVGT ISGNSGELTL SKRSTRTSFT FRKVRHSPCD CAFPSECDSQ QTQKEKSPPT
VGELGASTLE REYVHKVYDD IAGHFSSTRH TPWPKIGDFL ASLPKGSLVA DVGCGNGKYL
GVNKDLCMIG CDRSKNLVDI CRERTFEAFV CDALSVPFRA GAFDACISIA VIHHFATEER
RIAALQELIR LLRKGGKALI YVWALEQEYK KNKSKYLKES KTSQGPSSDA LGTNLAVKAP
LPIHTNRTSF HSQDLLVPWH LKPTNKSKVT PENKEQNEKE HGPDSVYHRF YHVFCEGELE
AMCNRLSNVA VQHSYHDQGN WCVILEKL
