GenomeNet

Database: UniProt
Entry: A0A0N4UDW3_DRAME
LinkDB: A0A0N4UDW3_DRAME
Original site: A0A0N4UDW3_DRAME 
ID   A0A0N4UDW3_DRAME        Unreviewed;       384 AA.
AC   A0A0N4UDW3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=tRNA-5-taurinomethyluridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011953};
DE            EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
GN   ORFNames=DME_LOCUS9280 {ECO:0000313|EMBL:VDN59307.1};
OS   Dracunculus medinensis (Guinea worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX   NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000553901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:DME_0000553901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN59307.1, ECO:0000313|Proteomes:UP000274756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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:0000256|ARBA:ARBA00003986}.
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:0000256|ARBA:ARBA00000897};
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family.
CC       {ECO:0000256|ARBA:ARBA00006191}.
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; UYYG01001179; VDN59307.1; -; Genomic_DNA.
DR   STRING; 318479.A0A0N4UDW3; -.
DR   WBParaSite; DME_0000553901-mRNA-1; DME_0000553901-mRNA-1; DME_0000553901.
DR   Proteomes; UP000038040; Unplaced.
DR   Proteomes; UP000274756; Unassembled WGS sequence.
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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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   InterPro; IPR046885; MnmA-like_C.
DR   InterPro; IPR046884; MnmA-like_central.
DR   InterPro; IPR023382; MnmA-like_central_sf.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR   NCBIfam; TIGR00420; trmU; 1.
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.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          7..50
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   384 AA;  43885 MW;  C963F9FF98A38667 CRC64;
     MKTIRRVVCA LSGGIDSAVA ALRLKQKGFD VVGLYMVNWD HLEEGQSECP QTQDKFVAKS
     ICDRLGIEFH VVNFVKIYWN DVFLYTINNY RKGRTVVPDI LCNRIIKFQH FHEYAINRLN
     ADAIATGHFA RTSFGDFLEN RSEKNKEVLL FRGSDPIKDQ SYFLSALTQD QLRRSMFPVG
     SLTKPQVRQI ASDANLNEVL NKPESMGICF IGKRKNFSDF IDQYIEPSPG PVRLIDSGET
     IWHHSGIHHF TIGKRVSVPH HQYRTHFGLF VVSLEYSTQT VWVCEGTYHP SLFATEFVIS
     QPVWIANSPF DFCGNCDEAN TEFSLQRTHK PHPCKLIRFT DNLVKLKPFY PVRAAAPGQI
     CAFYRDSECL GCAEIQYVLR TLAD
//
DBGET integrated database retrieval system