ID A0A3Q3G1T8_9LABR Unreviewed; 708 AA.
AC A0A3Q3G1T8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Alkylated DNA repair protein alkB homolog 8 {ECO:0000256|ARBA:ARBA00018748};
DE EC=2.1.1.229 {ECO:0000256|ARBA:ARBA00012808};
DE AltName: Full=Probable alpha-ketoglutarate-dependent dioxygenase ABH8 {ECO:0000256|ARBA:ARBA00031417};
DE AltName: Full=S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8 {ECO:0000256|ARBA:ARBA00032026};
DE AltName: Full=tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ABH8 {ECO:0000256|ARBA:ARBA00030990};
GN Name=ALKBH8 {ECO:0000313|Ensembl:ENSLBEP00000025073.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000025073.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000025073.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(carboxymethyl)uridine(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 Evidence={ECO:0000256|ARBA:ARBA00034996};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the alkB family.
CC {ECO:0000256|ARBA:ARBA00007879}.
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DR AlphaFoldDB; A0A3Q3G1T8; -.
DR STRING; 56723.ENSLBEP00000025073; -.
DR Ensembl; ENSLBET00000026344.1; ENSLBEP00000025073.1; ENSLBEG00000019152.1.
DR GeneTree; ENSGT00940000158563; -.
DR InParanoid; A0A3Q3G1T8; -.
DR OrthoDB; 5473013at2759; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0106335; F:tRNA (5-carboxymethyluridine(34)-5-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0043412; P:macromolecule modification; IEA:UniProt.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd12431; RRM_ALKBH8; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR13069:SF21; ALKYLATED DNA REPAIR PROTEIN ALKB HOMOLOG 8; 1.
DR PANTHER; PTHR13069; UNCHARACTERIZED; 1.
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; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022603};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 46..124
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 222..342
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 523..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 78476 MW; E9929706FF306A9C CRC64;
MDPSVENNVN GIRRSKEEKK ILKRQIKASY TLLKHEGITT TSQPTKNLVV ANGGLGNGVS
REELLSALKE MGELETLLMH PKKPFAFVTY RSEESAQKAY VHLNGQKLQC GENSVTLYLS
YVHSVTCEEE ASVSLPEGLT LVEDFVSQDE EDLLLAAVDW SSTNDDVSAQ KSLKHRKVKH
YGFEFRYDTN NVDKDKPLAS GIPQECLPVL ERCVKKAHIN ILPDQLTVNQ YESGQGIPPH
VDTHSAFEDT LLSLSLGART VMEFRHPDGH LVPVVLPPRS LLVMKGESRY LWTHGITPRK
YDMVPACDPQ SPALKTAEVG TPSNLTLRKR GTRTSFTFRK IRHKPCDCAF PSACDSQGAT
PPPPLLPCSH ADAALLEEEY VHRVYDAIAS HFSSTRHSPW PRVCHFLTSL PAGSVLADVG
CGNGKYLGVN PDVISVGCDR SSALVHICAE RGFQAFVSDA LSVPLRTASC DACISIAVIH
HFSTQDRRLA AVRELVRLLK PGGRALIYVW AFEQEYKKQR SKYLKDQNKE GSDVHSPTKN
TSEESQEPHG KSSRHLEDDN RPVNKIQDDS KVTDGKLSVH TNRTAFNTQD LLVPWHLKEG
KRRGEVEPVE TGRKDKMKDD SKKTSGKSCP TTSKDSKPIP SIGTTQSSTV KPKSESDSSP
APVFHRYYHV FQQGELEQLC GQVAGVEVQS SYHDQGNWCV ILEKAGTL
//
