ID U2QGP5_9BACT Unreviewed; 401 AA.
AC U2QGP5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=tRNA-uridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011949};
DE EC=2.8.1.13 {ECO:0000256|ARBA:ARBA00011949};
GN Name=trmU {ECO:0000313|EMBL:ERK40473.1};
GN ORFNames=HMPREF9135_1367 {ECO:0000313|EMBL:ERK40473.1};
OS Segatella baroniae F0067.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK40473.1, ECO:0000313|Proteomes:UP000016648};
RN [1] {ECO:0000313|EMBL:ERK40473.1, ECO:0000313|Proteomes:UP000016648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0067 {ECO:0000313|EMBL:ERK40473.1,
RC ECO:0000313|Proteomes:UP000016648};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) 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:ERK40473.1}.
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DR EMBL; AWEY01000004; ERK40473.1; -; Genomic_DNA.
DR AlphaFoldDB; U2QGP5; -.
DR PATRIC; fig|1115809.3.peg.151; -.
DR Proteomes; UP000016648; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 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; PTHR43052; -; 1.
DR PANTHER; PTHR43052:SF1; TRNA-5-TAURINOMETHYLURIDINE 2-SULFURTRANSFERASE; 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 Methyltransferase {ECO:0000313|EMBL:ERK40473.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016648};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ERK40473.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 249..311
FT /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT /evidence="ECO:0000259|Pfam:PF20259"
FT DOMAIN 321..399
FT /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20258"
SQ SEQUENCE 401 AA; 46042 MW; 3A59894F8CCD7971 CRC64;
MCALYLMYIN PRRLLPSFCV IPSFRNFAPM MITEEDKIDG LTVDELRQKR VAVLLSGGVD
SSVVVWEFAH LGLHPDCFYI KIGPEEKEEW DCSSEEDLEM ATAVAAKYGC RLQVVDCHKE
YWNQVTRYTM EKVKAGFTPN PDVMCNRLIK FGAFDEKMGH DYDLIATGHY ARTEVVNGEK
WLVTSPDPVK DQTDFLAQIY DWQLRKAIFP IGHHVKDEVR EIAEAEHLVN AKRRDSQGIC
FLGQINYNDY LRRYLGDCPG DVIELETGCK IGEHRALWYH TIGQRKGLGF GGGPWFVVKK
DVERNVLYVS HGYDPATAYK QDFKVHDFHF LTRKDVLPSG GKVTFKIRHT PEYHPAVVER
LSDHEFIIHS ETAIHGVAPG QFCVVYDERH HRCYGSAEIT F
//
