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Database: UniProt
Entry: U5H323_USTV1
LinkDB: U5H323_USTV1
Original site: U5H323_USTV1 
ID   U5H323_USTV1            Unreviewed;       411 AA.
AC   U5H323;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   13-SEP-2023, entry version 41.
DE   RecName: Full=tRNA-5-taurinomethyluridine 2-sulfurtransferase {ECO:0000256|ARBA:ARBA00011953};
DE            EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
GN   ORFNames=MVLG_01750 {ECO:0000313|EMBL:KDE08049.1};
OS   Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS   smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE08049.1};
RN   [1] {ECO:0000313|Proteomes:UP000017200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA   Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA   Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA   Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KDE08049.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE08049.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA   Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KDE08049.1, ECO:0000313|Proteomes:UP000017200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE08049.1}, and p1A1 Lamole
RC   {ECO:0000313|Proteomes:UP000017200};
RX   PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA   Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA   Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA   Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA   Hood M.E., Schultz D.J., Cuomo C.A.;
RT   "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT   lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT   fungus.";
RL   BMC Genomics 16:461-461(2015).
RN   [4] {ECO:0000313|EnsemblFungi:MVLG_01750T0}
RP   IDENTIFICATION.
RG   EnsemblFungi;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC       (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for
CC       the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of
CC       mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble
CC       position. ATP is required to activate the C2 atom of the wobble base.
CC       {ECO:0000256|ARBA:ARBA00003986}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-
CC         cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A +
CC         AMP + diphosphate + H(+) + L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:47040, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11726,
CC         Rhea:RHEA-COMP:11732, Rhea:RHEA-COMP:11733, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963,
CC         ChEBI:CHEBI:87171, ChEBI:CHEBI:87172, ChEBI:CHEBI:456215;
CC         EC=2.8.1.14; Evidence={ECO:0000256|ARBA:ARBA00000897};
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family.
CC       {ECO:0000256|ARBA:ARBA00006191}.
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DR   EMBL; AEIJ01000169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL541653; KDE08049.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5H323; -.
DR   STRING; 683840.U5H323; -.
DR   EnsemblFungi; MVLG_01750T0; MVLG_01750T0; MVLG_01750.
DR   HOGENOM; CLU_035188_1_2_1; -.
DR   InParanoid; U5H323; -.
DR   OMA; AVCTGHY; -.
DR   OrthoDB; 231303at2759; -.
DR   Proteomes; UP000017200; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0061708; F:tRNA-5-taurinomethyluridine 2-sulfurtransferase; IEA:UniProtKB-EC.
DR   GO; GO:1990799; P:mitochondrial tRNA wobble position uridine thiolation; IEA:EnsemblFungi.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017200};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KDE08049.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          244..304
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   DOMAIN          315..397
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20258"
SQ   SEQUENCE   411 AA;  46380 MW;  3D6B283F11120B12 CRC64;
     MRFTLARFKP NPTPLYPPLT AWNFPLRGSK IYVACSAGID SSVTARLLLE RDYDVRPVFM
     RNWDALDENS QHSGGCEWEK DWEQVQVLCK ESLGGVEPTL VDLSKQYWNE VFERSLGEWE
     RGVTPNPDVV CNQEIKFRTL PSILFDKDPN AYLATGHYAR LSPSSLDPLE PALHRGAYPL
     KDQSYYLSTS PVSALKRTLF PLGEYRKDEV KEMARIWGLP DKITERKESM GICFVGKKGK
     RFRHWLDAYL PPKPGHIVLT SGKIVGQHQG LWQYTIGEGA RLPGLPSRHF IGRKDRKNNE
     IVVVPEDSPI LRVVKLFTKD FKWLSSHHPP SEINSAEGFK VDAQTRSLQE RSLARSVVRR
     AGDYSLEIEL NEPLIGVSPG QAVVLYNGTW CLGGGTIEST TTLADLPQSS N
//
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