ID A0A452J3S9_9SAUR Unreviewed; 672 AA.
AC A0A452J3S9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000035089.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000035089.1}
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; A0A452J3S9; -.
DR STRING; 38772.ENSGAGP00000035089; -.
DR Ensembl; ENSGAGT00000039732.1; ENSGAGP00000035089.1; ENSGAGG00000024945.1.
DR Proteomes; UP000291020; 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; 2.60.120.1520; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 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:UP000291020};
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 43..123
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 221..338
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 556..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 76116 MW; 0B6C8F86A689462B CRC64;
MDSTGQNNLK RNKSEKKLLR KQIKARNTLM RHEGIDCVSH TTQNLVVANG GLGNGVNRHQ
LLSLVEECGL VEALLMPPNK PYSVVKYGST EEAKKAYDTL NGKEIMLEDS NQNVTLYVNF
VEKVHWEDII PISLPPGLMM VEELVSPEEE QKMLESIDWT ENEVIQNAQK SLKHRRVKHF
GYEFRYDNNN VDKDKPLPGG LPEICNMLLE KCLKQGYIKH KPDQLTINQY EPGQGIPPHI
DTHSAFEDEI TSLSLGAEIV MDFKHPDGRT VAVMLPQRSL LVMTGESRYL WTHGITPRKF
DIVHASERQK VGSVTPDVGD LTLNRRGTRT SFTFRKVRRS PCNCIYPSVC DSQQGHQREE
APLFHDSETQ ASKLEQAYVH KVYEEIAAHF SSTRHSPWPK IVEFLRTLPK GSIVADIGCG
NGKYLGINKD LYMIGCDRSQ NLVDICGEKK FQAFVCDALS VPVRNSSCDA CISIAVIHHF
STAERRLAAV RELARLLRSG GMALIYVWAM EQEYNKQKSK YLKEKRASKE KEEEINTDVA
WGLFCDQMHD NGSQDSACSD RVLNDSKDKG GNAKQGINSK LPVHTNRTSF RSQDVLVPWH
LKGGTNKKGE CVKALQLPAS SKELQEFSPV FHRYYHVFCE GELEAACKTL DCIRIQKSYY
DQGNWCVVLE KQ
//
