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Database: UniProt
Entry: D5AWN2_RICPP
LinkDB: D5AWN2_RICPP
Original site: D5AWN2_RICPP 
ID   D5AWN2_RICPP            Unreviewed;       358 AA.
AC   D5AWN2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 56.
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:ADE29821.1};
GN   Synonyms=mnmA {ECO:0000256|HAMAP-Rule:MF_00144};
GN   OrderedLocusNames=rpr22_CDS300 {ECO:0000313|EMBL:ADE29821.1};
OS   Rickettsia prowazekii (strain Rp22).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=449216 {ECO:0000313|EMBL:ADE29821.1, ECO:0000313|Proteomes:UP000006931};
RN   [1] {ECO:0000313|EMBL:ADE29821.1, ECO:0000313|Proteomes:UP000006931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rp22 {ECO:0000313|EMBL:ADE29821.1,
RC   ECO:0000313|Proteomes:UP000006931};
RX   PubMed=20368341; DOI=10.1101/gr.103564.109;
RA   Bechah Y., El Karkouri K., Mediannikov O., Leroy Q., Pelletier N.,
RA   Robert C., Medigue C., Mege J.L., Raoult D.;
RT   "Genomic, proteomic, and transcriptomic analysis of virulent and avirulent
RT   Rickettsia prowazekii reveals its adaptive mutation capabilities.";
RL   Genome Res. 20:655-663(2010).
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}.
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DR   EMBL; CP001584; ADE29821.1; -; Genomic_DNA.
DR   RefSeq; WP_004597398.1; NC_017560.1.
DR   AlphaFoldDB; D5AWN2; -.
DR   SMR; D5AWN2; -.
DR   GeneID; 57569433; -.
DR   KEGG; rpq:rpr22_CDS300; -.
DR   PATRIC; fig|449216.3.peg.312; -.
DR   HOGENOM; CLU_035188_0_1_5; -.
DR   OMA; AVCTGHY; -.
DR   Proteomes; UP000006931; Chromosome.
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:ADE29821.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00144};
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          207..270
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   DOMAIN          277..353
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20258"
FT   REGION          147..149
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   ACT_SITE        101
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   ACT_SITE        197
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         125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   SITE            126
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   SITE            337
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
SQ   SEQUENCE   358 AA;  39533 MW;  93BEA1C817561B24 CRC64;
     MATIVVAMSG GVDSSAVAAM LHEQGHNVIG ITLQLYDYGI AVGKKNACCA GQDIYDAKMV
     ANKLGIPHYV LDYENKFKES VIDNFVDSYL HGETPLPCVQ CNKSVKFRDL INTAKELGAD
     KLATGHYVRK INGYNGAELH TGLDTTKDQS YFLFTITREQ LEYLSFPLGG FTKYETRKLA
     SKFGLDIADK PDSQDICFVP DGNYKTVINK IRPEANTSGK IVHINGFELG EHSGIINYTI
     GQRRGLGIAY NEPLYVVKID PSNNIVYVGQ ESALHVHEFI IKDVNWLADE IKDHEKLAVD
     VKIRSTRPPC HAEISKLCND RIKVKFLSKE KAVAPGQACV IYAGERVLGG GWITSNIS
//
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