ID MTU1_CHICK Reviewed; 424 AA.
AC Q5ZKW0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 98.
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=RCJMB04_8p20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719974; CAG31633.1; -; mRNA.
DR RefSeq; NP_001026522.1; NM_001031351.1.
DR AlphaFoldDB; Q5ZKW0; -.
DR SMR; Q5ZKW0; -.
DR STRING; 9031.ENSGALP00000053750; -.
DR PaxDb; 9031-ENSGALP00000006683; -.
DR Ensembl; ENSGALT00000053602; ENSGALP00000053750; ENSGALG00000031922.
DR Ensembl; ENSGALT00010019693.1; ENSGALP00010011241.1; ENSGALG00010008230.1.
DR Ensembl; ENSGALT00015041607; ENSGALP00015024246; ENSGALG00015017044.
DR GeneID; 425909; -.
DR KEGG; gga:425909; -.
DR CTD; 55687; -.
DR VEuPathDB; HostDB:geneid_425909; -.
DR eggNOG; KOG2805; Eukaryota.
DR GeneTree; ENSGT00390000014323; -.
DR InParanoid; Q5ZKW0; -.
DR OMA; GRHDGLM; -.
DR OrthoDB; 231303at2759; -.
DR PhylomeDB; Q5ZKW0; -.
DR TreeFam; TF105611; -.
DR PRO; PR:Q5ZKW0; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000031922; Expressed in testis and 12 other cell types or tissues.
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: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..424
FT /note="Mitochondrial tRNA-specific 2-thiouridylase 1"
FT /id="PRO_0000248303"
FT REGION 97..99
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 172..174
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 343..344
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 403..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 231
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 128
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 276
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 376
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 102..231
FT /note="Alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 424 AA; 48370 MW; 0C9E55ED30F511C5 CRC64;
MLAAGRRVAC AVSGGVDSAV AALLLRRRGY QVTGVFMKNW DPLDEQGACS VDRDCEDAYR
VCQKLDIPFH QVSYVKEYWN EVFSDLLKEY ELGRTPNPDI VCNKHIKFNH FLHYAMDNLG
ADAIATGHYA RTSLEDEEVF QQKHTKRPRE LFRNRFEVRN TVKLLQGADL FKDQTFFLSQ
ISQDALRKTI FPLGDLTKSF VRKIASEHGL HHVLKKKEAC TTFPFQSMGV CFIGERNFEK
FLLEYLEPQP GNFVSIEDKK VMGTHKGWFL YTIGQRARLA GLQGAWFVVD KDVSTGDIFV
APSTDHPALF RDLLRTNRVH WIAEEPPAEL VRDKMMECHF RFRHQMALVP CVLTLNQDGS
VWVTLVKPAR ALTPGQFAVF YKGDECLGSG KILRLGPSVF TMQQGRNREE GTKKEDIDKV
EPAT
//
