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Database: UniProt
Entry: A0A1Y2T258_SYMTR
LinkDB: A0A1Y2T258_SYMTR
Original site: A0A1Y2T258_SYMTR 
ID   A0A1Y2T258_SYMTR        Unreviewed;       295 AA.
AC   A0A1Y2T258;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=tRNA-uridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011949};
DE            EC=2.8.1.13 {ECO:0000256|ARBA:ARBA00011949};
DE   Flags: Fragment;
GN   ORFNames=A6D92_15825 {ECO:0000313|EMBL:OTA40560.1};
OS   Symbiobacterium thermophilum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=2734 {ECO:0000313|EMBL:OTA40560.1, ECO:0000313|Proteomes:UP000194267};
RN   [1] {ECO:0000313|Proteomes:UP000194267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antunes L.P., Martins L.F., Pereira R.V., Thomas A.M., Barbosa D.,
RA   Nascimento L., Silva G.M., Condomitti G.W., Digiampietri L.A.,
RA   Lombardi K.C., Ramos P.L., Quaggio R.B., Oliveira J.C., Pascon R.C.,
RA   Cruz J.B., Silva A.M., Setubal J.C.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:OTA40560.1}.
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DR   EMBL; LWLV01001528; OTA40560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2T258; -.
DR   Proteomes; UP000194267; 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; 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; 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          181..245
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OTA40560.1"
FT   NON_TER         295
FT                   /evidence="ECO:0000313|EMBL:OTA40560.1"
SQ   SEQUENCE   295 AA;  33468 MW;  CB5B1F9806E453DF CRC64;
     MNTWTDDIPE EIQMNQHSGC CSLAAVEDAR SVAHKLGIPY YVMNFQGQFA RTVIDYFIEE
     YTRGRTPNPC IACNRYVKFS AFLEKARQLE CDYVATGHYA VIGRDDRFPG RWLLGKSADA
     RKDQTYVLHN LTQEALAHTL FPVGHMQKSE VRALAKKYGF VTADKPDSQE ICFVYDNDYG
     RFLKERVPEA IVPGPILNTR GEVIGQHQGL PLYTVGQRKG LGLTTRRPMY VVELDVERNA
     LIVGEAEETY RPGLIASDLN WIAIPELTEP RRCRAKIRRM APEADCTIYP LDDGT
//
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