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Database: UniProt
Entry: A0A0G0YL69_9BACT
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Original site: A0A0G0YL69_9BACT 
ID   A0A0G0YL69_9BACT        Unreviewed;       381 AA.
AC   A0A0G0YL69;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=tRNA-uridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011949};
DE            EC=2.8.1.13 {ECO:0000256|ARBA:ARBA00011949};
GN   ORFNames=UV01_C0010G0006 {ECO:0000313|EMBL:KKS37430.1};
OS   Parcubacteria group bacterium GW2011_GWA2_42_14.
OC   Bacteria.
OX   NCBI_TaxID=1618820 {ECO:0000313|EMBL:KKS37430.1, ECO:0000313|Proteomes:UP000034025};
RN   [1] {ECO:0000313|EMBL:KKS37430.1, ECO:0000313|Proteomes:UP000034025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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};
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:KKS37430.1}.
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DR   EMBL; LCCV01000010; KKS37430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0YL69; -.
DR   STRING; 1618820.UV01_C0010G0006; -.
DR   PATRIC; fig|1618820.3.peg.969; -.
DR   Proteomes; UP000034025; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; 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: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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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          240..297
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   DOMAIN          306..379
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20258"
SQ   SEQUENCE   381 AA;  42102 MW;  56A9D49CFC0F51F0 CRC64;
     MPETVQKKDS PLSKTTKNVV FLMLSGGKDS GVAARLLKDE GKEVIGFFIK GWAPTGLKCL
     EPPEMRDAAE IARVVGIEFF PILNWSEHFY NAVFDPMLSG YLSGITPNPD TLCNREIKFG
     LFAKFAFGRG ADYIASGHYV RKNDNPLQLL VARDERKDQS YFLYDLKTDI LERSLFPIGN
     YVKSEEVIPM ARSFGLPQRV IEKRPTRDIC FLLKSEEDAT DGGRIGMEKL LRLEGEKRGI
     KFSSGPVIHE KTGKVVGEHN GVSLFAVTIG QRHGLGLAGG KLLYVSRKDI LKNAFYVNSE
     KPSSPEVVVK NLNWISGAPD FGKKLSAKIR TPQKAQSCRV EKIGEDEIRV KFDTPQNSVA
     PGQACVLYDG EVVLGGGIIV S
//
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