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Database: UniProt
Entry: U4QTD9_9BACT
LinkDB: U4QTD9_9BACT
Original site: U4QTD9_9BACT 
ID   U4QTD9_9BACT            Unreviewed;       304 AA.
AC   U4QTD9;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=tRNA-uridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011949};
DE            EC=2.8.1.13 {ECO:0000256|ARBA:ARBA00011949};
GN   ORFNames=C75L2_00160011 {ECO:0000313|EMBL:EIJ77117.1};
OS   Leptospirillum sp. Group II 'C75'.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1159328 {ECO:0000313|EMBL:EIJ77117.1, ECO:0000313|Proteomes:UP000016760};
RN   [1] {ECO:0000313|EMBL:EIJ77117.1, ECO:0000313|Proteomes:UP000016760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22539719; DOI=10.1126/science.1218389;
RA   Denef V.J., Banfield J.F.;
RT   "In situ evolutionary rate measurements show ecological success of recently
RT   emerged bacterial hybrids.";
RL   Science 336:462-466(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in
CC         tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-
CC         cysteinyl-[protein]; Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131,
CC         Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11727, Rhea:RHEA-COMP:11728,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, ChEBI:CHEBI:87170,
CC         ChEBI:CHEBI:456215; EC=2.8.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001042};
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DR   EMBL; JH660553; EIJ77117.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4QTD9; -.
DR   HOGENOM; CLU_035188_0_0_0; -.
DR   Proteomes; UP000016760; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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   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   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Methyltransferase {ECO:0000313|EMBL:EIJ77117.1};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EIJ77117.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
SQ   SEQUENCE   304 AA;  34699 MW;  83C312FC503D9D0D CRC64;
     MKSRVLVGLS GGVDSTVAAL LLKEAGFDVY GAIVEIWSEN SSGGRSGEER EKPWFERACC
     HLPMVKFLCE EYLHIPYVQI DQKQNFQEKI VDVFREGYHN GVTPNPCTDC NAEIKIKTLI
     DWAEQQKISY VATGHYAKNH YSVQNRLWGI AQALDRKKDQ SYFLSRVPEH VLRKVLFPLG
     HWTKDKVREF ARSKKIPVEE MVENMEACFL SAKNVTSFLK REEEVHSSGN WKVTDMKGEK
     IGEIPTGIGL TKGQRKGIGV ANAERMYVKK VDVHNKVVIM GSKKDILNRN FRIRDPLGPL
     FQKK
//
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