MTU1_DANRE
ID MTU1_DANRE Reviewed; 416 AA.
AC Q503J2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Mitochondrial tRNA-specific 2-thiouridylase 1;
DE EC=2.8.1.14 {ECO:0000250|UniProtKB:Q12093};
GN Name=trmu; Synonyms=mtu1; ORFNames=zgc:110555;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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:O75648}.
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; BC095308; AAH95308.1; -; mRNA.
DR RefSeq; NP_001018435.1; NM_001020599.1.
DR AlphaFoldDB; Q503J2; -.
DR SMR; Q503J2; -.
DR STRING; 7955.ENSDARP00000064218; -.
DR PaxDb; Q503J2; -.
DR GeneID; 553625; -.
DR KEGG; dre:553625; -.
DR CTD; 55687; -.
DR ZFIN; ZDB-GENE-050522-540; trmu.
DR eggNOG; KOG2805; Eukaryota.
DR InParanoid; Q503J2; -.
DR OrthoDB; 697006at2759; -.
DR PhylomeDB; Q503J2; -.
DR PRO; PR:Q503J2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0070903; P:mitochondrial tRNA thio-modification; IMP:ZFIN.
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 2: Evidence at transcript level;
KW ATP-binding; Disulfide bond; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..416
FT /note="Mitochondrial tRNA-specific 2-thiouridylase 1"
FT /id="PRO_0000349874"
FT REGION 96..98
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 171..173
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 334..335
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 397..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 267
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 367
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 101..222
FT /note="Alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 416 AA; 47564 MW; 3B85AF29D89B6A15 CRC64;
MGVLRHVVCA MSGGVDSSVS ALLLKRMGYH VTGVFMKNWD SQEEKGLCSS DRDCEDAYKV
CKMLDIPFHE VSYVKEYWHE VFSNLLWEYE RGRTPNPDII CNKHIKFKHF YQYAVNTLGA
DAMATGHYAR TSQEDEEVFQ QKLTEAPKSL FRDRFEIRKP VRLYQGADLL KDQTFFLSQI
SQDALRHTLF PLAGLTKGYV KKIAAEAGFQ HVLKKKESMG ICFIGKRDFE NFILEYLEPR
PGNFVSIEDG QIMGKHKGWF TLTLGQRARI GGRADAWFVV DKDVTTADVF VCPSTFHPAL
FRDTLQTDRF HWIAEEPPAE LVHTQMMDCH FCFNNRMPLT PCTVTLNLDG SVWVMVKEPM
RGMATGQFAV LYKGHECLGS GKIIRLGPTK FALQKDQSNT NCLHKDTNQQ HPEPHS
