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Database: UniProt
Entry: A0A1Z5JEN3_FISSO
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ID   A0A1Z5JEN3_FISSO        Unreviewed;       596 AA.
AC   A0A1Z5JEN3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=tRNA-5-taurinomethyluridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011953};
DE            EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
GN   ORFNames=FisN_24Hh037 {ECO:0000313|EMBL:GAX12463.1};
OS   Fistulifera solaris (Oleaginous diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC   Fistulifera.
OX   NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX12463.1, ECO:0000313|Proteomes:UP000198406};
RN   [1] {ECO:0000313|EMBL:GAX12463.1, ECO:0000313|Proteomes:UP000198406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX12463.1,
RC   ECO:0000313|Proteomes:UP000198406};
RX   PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA   Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA   Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA   Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT   "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT   by the genome and transcriptome.";
RL   Plant Cell 27:162-176(2015).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAX12463.1}.
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DR   EMBL; BDSP01000052; GAX12463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5JEN3; -.
DR   InParanoid; A0A1Z5JEN3; -.
DR   OrthoDB; 231303at2759; -.
DR   Proteomes; UP000198406; 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; 3.90.1010.10; -; 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; IPR003808; Fe-S_metab-assoc_dom.
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; PTHR43052; -; 1.
DR   PANTHER; PTHR43052:SF1; TRNA-5-TAURINOMETHYLURIDINE 2-SULFURTRANSFERASE; 1.
DR   Pfam; PF02657; SufE; 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   SUPFAM; SSF82649; SufE/NifU; 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:UP000198406};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAX12463.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..596
FT                   /note="tRNA-5-taurinomethyluridine 2-sulfurtransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012554795"
FT   DOMAIN          81..181
FT                   /note="Fe-S metabolism associated"
FT                   /evidence="ECO:0000259|Pfam:PF02657"
FT   DOMAIN          413..479
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   DOMAIN          492..574
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20258"
SQ   SEQUENCE   596 AA;  66412 MW;  E918E2D617753898 CRC64;
     MALSSWLQLA LFLALGTFPV NSFSVSHLET KLNWWKNRFS QMSLEDISKD LVQHGYQWKK
     KQQQHQLEKK SQETYTATGT TTTTPFVKVP GCTANVHIQL ILTSDASTTI NSRTIQSLEG
     TADALVSQGL VAVIASCVEQ ESEDAIGQIS AESITTRLGL QQHLSPGRND GVASLWRTLQ
     QSLQSSSPAS FITSTEPSTQ SQQPSVALLL SGGVDSSVAL RLLLQQNYRV TAFYLKIWLQ
     DENAHLGGTC PWEEDWKICQ QVCEQANVPL QAISLQQEYH ERVVEYAMEQ ASLGRTPNPD
     ILCNSRIKFG CFYDVLMSQQ AEQFDYIATG HYARVERDDD DASARLFRAP DAVKDQSYFL
     CTLTQEQLQK TLFPLGHLEK AQVRQLADEF ELPNRHRPDS QGLCFLGQVK FDQFLESYLG
     TQPGSVVDAV TGDNIGQHQG VWFHTIGQRK GIGKALNPQA TARGPWYVVS KDPAQRIVYC
     TNQYELFDAQ RKHVELEDIT WMSGQLPAMV SGGNACHLTM KLRHGPRLAR GLLQLNNADF
     SKGTVELEQM DSGLAPGQYV VFYADDGECL GSGIMSESQW NRPICLETQA VEQMTS
//
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