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Database: UniProt
Entry: A0A1E3QPL3_9ASCO
LinkDB: A0A1E3QPL3_9ASCO
Original site: A0A1E3QPL3_9ASCO 
ID   A0A1E3QPL3_9ASCO        Unreviewed;       359 AA.
AC   A0A1E3QPL3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=tRNA-5-taurinomethyluridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011953};
DE            EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
GN   ORFNames=BABINDRAFT_171760 {ECO:0000313|EMBL:ODQ79601.1};
OS   Babjeviella inositovora NRRL Y-12698.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX   NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ79601.1, ECO:0000313|Proteomes:UP000094336};
RN   [1] {ECO:0000313|Proteomes:UP000094336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV454432; ODQ79601.1; -; Genomic_DNA.
DR   RefSeq; XP_018984929.1; XM_019130837.1.
DR   AlphaFoldDB; A0A1E3QPL3; -.
DR   STRING; 984486.A0A1E3QPL3; -.
DR   GeneID; 30148690; -.
DR   OrthoDB; 231303at2759; -.
DR   Proteomes; UP000094336; 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; 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.
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:UP000094336};
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          198..265
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   DOMAIN          277..354
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20258"
SQ   SEQUENCE   359 AA;  40394 MW;  6E8DA75B630EB9CF CRC64;
     MSSGVDSSVC AALYAAKYKN VKGVYMANWS QTAKCTEAEW NDVQRVCEKL RIPCERVNFE
     KEYWMDVFQP MVEMYERGLT PNPDVGCNRY VKFGKMIEHL TRTRTEHKNW WLATGHYARM
     LTHKESGEPH LLRGSYTNKD QSYYLSMLPK AAMGRLLFPI GHYTKPEVRE LAKSFELPTA
     EKPDSVGLCF VSQDGSFRDF LNDYISPKPG NIITEDGTVH GRHNGIWHAT IGQKSGISLP
     QGDPRYKGVW FVSAKRYKTN EIVIVKGGDN AALFSRMVVA SDWNWVGEMS KEKMPPSGEL
     SVQYRSLQAP CAVESFVVKD GTVECRFKEG ARAIAPGQNL VLYHGERVLG AGLIVGATE
//
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