ID A0A182ECF6_ONCOC Unreviewed; 577 AA.
AC A0A182ECF6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=NOO_LOCUS5750 {ECO:0000313|EMBL:VDK79224.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t05750-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t05750-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK79224.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) 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; UYRW01001611; VDK79224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182ECF6; -.
DR STRING; 42157.A0A182ECF6; -.
DR WBParaSite; nOo.2.0.1.t05750-RA; nOo.2.0.1.t05750-RA; nOo.2.0.1.g05750.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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 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; 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 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000271087};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 33..94
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 206..311
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 577 AA; 66418 MW; DCB15FF865D46284 CRC64;
MMDQSKISRK LRKCLLQLQK HDPDVEISSI PSKILFVANS SPLCGISYNE LERIFNQFGE
NCDFVVFQSQ RSYSFVIFHT VATAQSAYQK LHGQVPSGLN SNALPFYIVF VKNVPTIKRT
EPLYKPNNLR LLPDFITADE EAVLISVIQD YMPSGRTLKS RKVIHFGFEF NYDDNMACEH
PSSNPIPSAC QPIIDRMLDA GIFREKPDQL TVNIYEPGNG IPSHVDTHSA FSDTIASLSL
LSDLVMEFRD FANTSIIYDV LLPRFSLTVM QGESRYRWKH GIAKRKYDIN PMTNRLTPRQ
LRVSFTFRKV IREKCQCAFI EYCDWDRNGT MKVPDNDEYG AAIEKQYVSA VYESIANHFD
TTRHAQWNGV AKFLANFEPG TVVYDIGCGN GKYLKLDDAL IKIGCDLCSN LCRIANQKQC
NVLRADILSL PFKNSTAGAV LCIAVIHHLT TRMRRLRAIQ EIIRVLKSDG QACITVWAYE
QKLCDEPSEY LKMRRKKRDV QMNRRDSHGR LRVHEGREFT QPDMLVPFQN ADGSRFLRYY
HLFRDFELED LINVVGGCII EKYFYEQGNW IAYIRKT
//
