ID MTU1_RAT Reviewed; 441 AA.
AC B1WC37;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, 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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 a 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC161991; AAI61991.1; -; mRNA.
DR RefSeq; XP_006242226.1; XM_006242164.3.
DR AlphaFoldDB; B1WC37; -.
DR SMR; B1WC37; -.
DR STRING; 10116.ENSRNOP00000061254; -.
DR iPTMnet; B1WC37; -.
DR PhosphoSitePlus; B1WC37; -.
DR PaxDb; 10116-ENSRNOP00000061254; -.
DR PeptideAtlas; B1WC37; -.
DR Ensembl; ENSRNOT00000065283.4; ENSRNOP00000061254.1; ENSRNOG00000016465.8.
DR Ensembl; ENSRNOT00055055865; ENSRNOP00055046026; ENSRNOG00055032359.
DR Ensembl; ENSRNOT00060044838; ENSRNOP00060037188; ENSRNOG00060025893.
DR Ensembl; ENSRNOT00065057424; ENSRNOP00065047265; ENSRNOG00065033401.
DR AGR; RGD:1311229; -.
DR CTD; 55687; -.
DR RGD; 1311229; Trmu.
DR eggNOG; KOG2805; Eukaryota.
DR GeneTree; ENSGT00390000014323; -.
DR HOGENOM; CLU_035188_1_1_1; -.
DR InParanoid; B1WC37; -.
DR OMA; GRHDGLM; -.
DR OrthoDB; 231303at2759; -.
DR PhylomeDB; B1WC37; -.
DR TreeFam; TF105611; -.
DR PRO; PR:B1WC37; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000016465; Expressed in pancreas and 20 other cell types or tissues.
DR ExpressionAtlas; B1WC37; baseline and differential.
DR Genevisible; B1WC37; RN.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
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:UniProtKB-EC.
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; Adenine nucleotide alpha hydrolases-like domains; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR InterPro; IPR046885; MnmA-like_C.
DR InterPro; IPR046884; MnmA-like_central.
DR InterPro; IPR023382; MnmA-like_central_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR PANTHER; PTHR11933:SF5; MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1; 1.
DR PANTHER; PTHR11933; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE; 1.
DR Pfam; PF03054; tRNA_Me_trans; 1.
DR Pfam; PF20258; tRNA_Me_trans_C; 1.
DR Pfam; PF20259; tRNA_Me_trans_M; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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..441
FT /note="Mitochondrial tRNA-specific 2-thiouridylase 1"
FT /id="PRO_0000349873"
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 358..359
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 421..441
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 291
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 391
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 101..222
FT /note="Alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 441 AA; 49724 MW; 13B09AFB51A73942 CRC64;
MSALRHVVCA LSGGVDSAVA ALLLRRRGYQ VTGVFMKNWD SLDEQGICAA DKDCEDAYKV
CQILDIPFHQ VSYVKEYWND VFSDFLNEYE KGRTPNPDIS CNKHIKFSCF HHYAVDNLGA
DAVATGHYAR TSLEDEEVFE QKHTKRPDGL FRNRFEVRNP VKLLQAADSF KDQTFFLSQV
SQDALRRTIF PLGELTKDFV KKIAAENRLH HVLQKKESMG ICFIGKRNLE HFLLQVSVSD
VSGGLLWAGA PVVMKPVFQY LQPRPGKFIS IEDNRVLGTH KGWFLYTLGQ RAKISGLSEP
WYVVEKDGTK GDVLVAPRVD HPALYRDLLR TNRVHWIAEE PPAALVRDKM MECHFRFRHQ
MALVPCVLTL NQDGTVWVTA VKAVRGLALG QFAVFYKGEE CLGSGKILRL GPSAYTLQKG
KNRTRVAPEV SSDSPGLHPT S
//
