MTU1_CAEEL
ID MTU1_CAEEL Reviewed; 375 AA.
AC Q17440;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable mitochondrial tRNA-specific 2-thiouridylase 1;
DE EC=2.8.1.14 {ECO:0000250|UniProtKB:Q12093};
GN Name=mttu-1 {ECO:0000312|WormBase:B0035.16};
GN ORFNames=B0035.16 {ECO:0000312|WormBase:B0035.16};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for
CC the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of
CC mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble
CC position. ATP is required to activate the C2 atom of the wobble base.
CC {ECO:0000250|UniProtKB:Q12093}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-
CC cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A +
CC AMP + diphosphate + H(+) + L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:47040, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11726,
CC Rhea:RHEA-COMP:11732, Rhea:RHEA-COMP:11733, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963,
CC ChEBI:CHEBI:87171, ChEBI:CHEBI:87172, ChEBI:CHEBI:456215;
CC EC=2.8.1.14; Evidence={ECO:0000250|UniProtKB:Q12093};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- MISCELLANEOUS: During the reaction, ATP is used to activate the C2 atom
CC of U34 by adenylation. After this, the persulfide sulfur on the
CC catalytic cysteine is transferred to the C2 atom of the wobble base
CC (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). The reaction
CC probably involves hydrogen sulfide that is generated from the
CC persulfide intermediate and that acts as nucleophile towards the
CC activated C2 atom on U34. Subsequently, a transient disulfide bond is
CC formed between the two active site cysteine residues (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000305}.
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DR EMBL; Z73102; CAA97418.2; -; Genomic_DNA.
DR PIR; T18663; T18663.
DR RefSeq; NP_502120.1; NM_069719.3.
DR AlphaFoldDB; Q17440; -.
DR SMR; Q17440; -.
DR STRING; 6239.B0035.16; -.
DR PaxDb; Q17440; -.
DR EnsemblMetazoa; B0035.16.1; B0035.16.1; WBGene00007114.
DR GeneID; 178038; -.
DR KEGG; cel:CELE_B0035.16; -.
DR UCSC; B0035.16; c. elegans.
DR CTD; 178038; -.
DR WormBase; B0035.16; CE26926; WBGene00007114; mttu-1.
DR eggNOG; KOG2805; Eukaryota.
DR GeneTree; ENSGT00390000014323; -.
DR HOGENOM; CLU_035188_1_0_1; -.
DR InParanoid; Q17440; -.
DR OMA; VHLLCEQ; -.
DR OrthoDB; 697006at2759; -.
DR PhylomeDB; Q17440; -.
DR PRO; PR:Q17440; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00007114; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; ISS:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061708; F:tRNA-5-taurinomethyluridine 2-sulfurtransferase; IEA:RHEA.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 2.30.30.280; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR InterPro; IPR023382; Adenine_a_hdrlase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR TIGRFAMs; TIGR00420; trmU; 1.
PE 3: Inferred from homology;
KW ATP-binding; Disulfide bond; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..375
FT /note="Probable mitochondrial tRNA-specific 2-thiouridylase
FT 1"
FT /id="PRO_0000121707"
FT REGION 94..96
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 154..156
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 319..320
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 205
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 125
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 250
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 351
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 99..205
FT /note="Alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 42795 MW; CE7A5EB4B7A313F4 CRC64;
MPRVVIGMSG GVDSAVSAFL LKKRGFDVIG LHMINWDVQE EGTSHCPRSK DESDARNVCD
RLNIPFHTVN FVKEYWNDVF LKFLENYKNG RTTVPDIDCN QSIKFDVFHK IAREKFNADF
IATGHYATTN FGDFQQNAKD SDEIRLFSGK DPLKDQTFFL CTVNQEQLKR AMFPLGSLQK
SEVKRIAEEQ GFQEVAKKPE SMGICFIGKK KRFSDFLDEY IEPKPGRILL KNGSEIGNHH
GIHQFTIGKR INGKYLEARS HLGFFVSHIH SDTGDIIACE GSHHPDLYAS RFLINHPKWI
RTFDPFNRIS SNNFLCRIQR THPPIPCVAE KQEQFLSVIP RLALRATAPG QMCVFYNTKN
ECLGGGEIMN IQETL
