ID A0A060XPM0_ONCMY Unreviewed; 683 AA.
AC A0A060XPM0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ORFNames=GSONMT00003578001 {ECO:0000313|EMBL:CDQ81421.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ81421.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ81421.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ81421.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; FR905758; CDQ81421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060XPM0; -.
DR STRING; 8022.A0A060XPM0; -.
DR PaxDb; 8022-A0A060XPM0; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:InterPro.
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; 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 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; PF09004; ALKBH8_N; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF00076; RRM_1; 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:UP000193380};
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 45..112
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 220..368
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 285..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 76538 MW; 3E6121DEF7B0BE97 CRC64;
MESCSENVKA VRRSKEEKKL LRKQIKASHT LLKHEGISTV SQPTKSLVVA NGGLGNGVSR
EQLQDVLEEV GEVEILVMPP HKPYALVTYR SEVSAQRGHA LNGRQLQRGD QIVTLYLSYV
NTVDSELWGC VDLPPGLVLV EEFVSPEEEA LLLDAIDWTS HDEDVTVQKV LKHRRVKHFG
YEFRYDNNNV DKDKPLPGGL PQVCVPVLER CVRDRHTEVM PDQLTVNQYQ SGQGIPPHVD
THSAFEDLIL SLSLGAKVHL QSVLMSSQNI KSILCPPPFL STHTHTHTHY SGEDGRERAD
TYGPTGKREM ERERCFLWFS RITPRKFDVV PACDPKSPAA VTSDLSNHSN LTLSRRGTRT
SLTFRKVRRT PCDCGYPSAC DSQQPPAPPS PPFLPRSQTD ACRLEAEFVH RVYEEIACHF
SSTRHSPWPR VCHFLSSLEP GSILADVGCG NGKYLGVNPD VIAVGCDRSS ALVQICSERG
FQAFVSDALN VPLRSDTCDA CISIAVIHHL STQKRRQAVV EELVRLLRPG GQALIYVWAV
EQEYNKQKSK YLKETRQQGP TRDSTDHNNQ ESKTQDLSGI ATDCTKVHRE TESPAKLSVH
INRTAFNSQD LLVPWHLKGS KNTLDPPTEA QAPAPSPVFH RYYHVFQKGE LEELCVRVRG
VAIQRSYHDQ GNWCVILKKT GDR
//
