ALKB8_MACFA
ID ALKB8_MACFA Reviewed; 664 AA.
AC Q95K79;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
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; ORFNames=QtrA-10552;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RX PubMed=11806829; DOI=10.1186/gb-2001-3-1-research0006;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Prediction of unidentified human genes on the basis of sequence similarity
RT to novel cDNAs from cynomolgus monkey brain.";
RL Genome Biol. 3:RESEARCH0006.1-RESEARCH0006.5(2002).
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; AB063089; BAB60797.1; -; mRNA.
DR RefSeq; NP_001306286.1; NM_001319357.1.
DR AlphaFoldDB; Q95K79; -.
DR SMR; Q95K79; -.
DR STRING; 9541.XP_005579574.1; -.
DR GeneID; 102129238; -.
DR CTD; 91801; -.
DR eggNOG; KOG1331; Eukaryota.
DR eggNOG; KOG4176; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
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_0000337126"
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 REGION 516..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 75189 MW; D2411317E065B2B2 CRC64;
MDSSHQSNYK LSKTEKKFLR KQIKARHTLL RHEGIETVSY ATQSLVVANG GLGNGVSRNQ
LLPVLEKCGL VDALLMPPNK PYSFARYKTT EESKRAYVTL NGKEVVDDLG QKIILYLNFV
EKAQWKELRP QALPPGLMVV EEIISSEEEK MLLESVDWTE DTDNQNSQKS LKHRRVKHFG
YEFHYENNNV DKDKPLPGGL PDICDSFLEK WLREGYIKHK PDQMTINQYE PGQGIPAHID
THSAFEDEIV SLSLGSEIVM DFKHPDGTAV PVMLPRRSLL VMTGESRYLW THGITCRKFD
TVQASENHKS GIITSDVGDL TLSKRGLRTS FTFRKVRQTP CNCSYPLVCD SQRKETPPSF
PESDEEASRL EQEYVHQVYE EIAGHFSSTR HTPWPHIVEF LKALPSGSIV ADIGCGNGKY
LGVNKELYMV GCDRSQNLVD ICRERQFQAF VCDALAVPVR SGSCDACISI AVIHHFATAE
RRVAALQEIV RLLRPGGKAL IYVWAMEQEY NKQKSKYLKG NRNSQGKKEE MNSDTSVQRS
LVEQMPDMGS RDSASSVPRI NDSQEGGCNS RQVSNSKLPI HVNRTSFYSQ DMLVPWHLKG
NPDKGKPVEP FGPIGSQDPS PVFHRYYHVF REGELEALCR TVSDVRILQS YYDQGNWCVI
LQKA
