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Database: UniProt
Entry: E0E298_9FIRM
LinkDB: E0E298_9FIRM
Original site: E0E298_9FIRM 
ID   E0E298_9FIRM            Unreviewed;       350 AA.
AC   E0E298;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000256|HAMAP-Rule:MF_00144};
DE            EC=2.8.1.13 {ECO:0000256|HAMAP-Rule:MF_00144};
GN   Name=trmU {ECO:0000313|EMBL:EFM64981.1};
GN   Synonyms=mnmA {ECO:0000256|HAMAP-Rule:MF_00144};
GN   ORFNames=HMPREF0634_1466 {ECO:0000313|EMBL:EFM64981.1};
OS   Peptostreptococcus stomatis DSM 17678.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptostreptococcus.
OX   NCBI_TaxID=596315 {ECO:0000313|EMBL:EFM64981.1, ECO:0000313|Proteomes:UP000003244};
RN   [1] {ECO:0000313|EMBL:EFM64981.1, ECO:0000313|Proteomes:UP000003244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17678 {ECO:0000313|EMBL:EFM64981.1,
RC   ECO:0000313|Proteomes:UP000003244};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC       (U34) of tRNA, leading to the formation of s(2)U34. {ECO:0000256|HAMAP-
CC       Rule:MF_00144}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00144};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00144}.
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000256|HAMAP-
CC       Rule:MF_00144}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00144}.
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:EFM64981.1}.
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DR   EMBL; ADGQ01000034; EFM64981.1; -; Genomic_DNA.
DR   RefSeq; WP_007788927.1; NZ_ADGQ01000034.1.
DR   AlphaFoldDB; E0E298; -.
DR   STRING; 596315.HMPREF0634_1466; -.
DR   eggNOG; COG0482; Bacteria.
DR   OrthoDB; 9800696at2; -.
DR   Proteomes; UP000003244; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00144}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00144};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Methyltransferase {ECO:0000313|EMBL:EFM64981.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00144}; Reference proteome {ECO:0000313|Proteomes:UP000003244};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00144};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00144};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00144};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_00144}.
FT   DOMAIN          201..264
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   DOMAIN          272..349
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20258"
FT   REGION          142..144
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   REGION          300..301
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   ACT_SITE        94
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   ACT_SITE        192
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   BINDING         7..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   SITE            119
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   SITE            333
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
SQ   SEQUENCE   350 AA;  39301 MW;  B7F9F49C2606ACEC CRC64;
     MKRVLLGMSG GVDSSVAAFL LQKEGYEVVG ATMALWDFKD GNKDTSIEDA RVVCNKLKID
     HHVLDFREDF KDLVVDNFID EYFAGKTPNP CVFCNKTIKF GLLFDKAREL GCDYVATGHY
     ALVDFNEKSG KYEIKKASSD SKDQTYVLYN LNQEKLARTL FPIGKYDKDT IRDMAKEIGL
     EVHNKPDSQD ICFIPDHDYE AFLKENSKKK VEVGNFVDRS GKVLGRHKGI ISYTIGQRKG
     LGITFGKPTY VVAINGQDKS IVLGDNDDLF KTSLTARDVN FVEWSQDEVV GPIDVYAKVR
     YAAKPAQAKV TYIGKYRVRV DFVEPQRAIT SGQSVVFYSE DRLLGGGIIE
//
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