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Database: UniProt
Entry: U3J8C5_ANAPP
LinkDB: U3J8C5_ANAPP
Original site: U3J8C5_ANAPP 
ID   U3J8C5_ANAPP            Unreviewed;       618 AA.
AC   U3J8C5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 2.
DT   27-MAR-2024, entry version 71.
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:ENSAPLP00000015753.2};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000015753.2, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000015753.2, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000015753.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; U3J8C5; -.
DR   Ensembl; ENSAPLT00000016554.2; ENSAPLP00000015753.2; ENSAPLG00000015851.2.
DR   GeneTree; ENSGT00940000158563; -.
DR   HOGENOM; CLU_029501_4_0_1; -.
DR   Proteomes; UP000016666; Chromosome 1.
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   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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016666};
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          1..61
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          166..284
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          466..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  69651 MW;  35945C9366610E94 CRC64;
     MNRKQLLKTV EEYGLVEALL MPPNKPYSFV KYGSTEEAKK AFDALNGKEL MLGDSGQNVV
     LYSNFVEKVF WKNAVPTNLP PGLTVIEKVV SPEEERRMLE SIDWIGDEDA QNAQKTLKHR
     KVKHFGYEFR YDNNNVDKDK PLPGGLPEIC SLFLEKCLKQ GYIKHKPDQL TVNQYEPGQG
     IPPHIDTHSA FEDEIISLSL GAEIVMDFKH PDGHTVAVLL PRCSLLVMSG ESRYLWTHGI
     TPRKYDIIQA SELGQKVGTI TADVGDITLN QRKTRTSFTF RKVRRSPCNC IYPSVCDSQK
     GQQRQVQPSF PHNEMEASEL EQEYVHKVYE EIATHFSSTR HSPWPRIVEF LRSLPEGSIV
     ADVGCGNGKY LGINKDLYMI GCDRSKNLVD ICGEKNFQAF VGDALSVPMR SGSCDACISI
     AVIHHFSTAE RRLAALRELA RLLRPGGTAL IYVWAMEQEY KNQKSKYLKE KHGNKDKEEE
     ISSGMAQRLP GDQMPESSSQ DSACTDQLLD NSKDKGCGAK PVADCRLPVH TNRTSFHSQD
     LLVPWHLKGG TKKRRESVET VLFPAGSKES QGPSPVFHRY YHVFCEGELE AACRSLDGVR
     VQKSYYDQGN WCVVLEKL
//
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