ID F7D8I5_CALJA Unreviewed; 421 AA.
AC F7D8I5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Mitochondrial tRNA-specific 2-thiouridylase 1 {ECO:0000256|ARBA:ARBA00018888};
DE EC=2.8.1.14 {ECO:0000256|ARBA:ARBA00011953};
GN Name=TRMU {ECO:0000313|EMBL:JAB37176.1,
GN ECO:0000313|Ensembl:ENSCJAP00000065010.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB37176.1};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000065010.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB37176.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:JAB47273.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB24085.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB37176.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000065010.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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; GAMR01009847; JAB24085.1; -; mRNA.
DR EMBL; GAMQ01004675; JAB37176.1; -; mRNA.
DR EMBL; GAMP01005482; JAB47273.1; -; mRNA.
DR RefSeq; XP_002743906.1; XM_002743860.3.
DR STRING; 9483.ENSCJAP00000065010; -.
DR Ensembl; ENSCJAT00000081646.3; ENSCJAP00000065010.1; ENSCJAG00000000198.5.
DR GeneID; 100387554; -.
DR KEGG; cjc:100387554; -.
DR CTD; 55687; -.
DR eggNOG; KOG2805; Eukaryota.
DR GeneTree; ENSGT00390000014323; -.
DR HOGENOM; CLU_035188_1_1_1; -.
DR OMA; GRHDGLM; -.
DR OrthoDB; 231303at2759; -.
DR TreeFam; TF105611; -.
DR Proteomes; UP000008225; Chromosome 1.
DR Bgee; ENSCJAG00000000198; Expressed in kidney and 6 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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: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 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 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 2: Evidence at transcript level;
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:UP000008225};
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 230..292
FT /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT /evidence="ECO:0000259|Pfam:PF20259"
FT DOMAIN 303..383
FT /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20258"
FT REGION 394..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 47626 MW; 824F7527A42DDC8E CRC64;
MQAARHVVCA LSGGVDSAVA ALLLKRRGYQ VTGVFMKNWD LLDEHGVCAA DKDCEDAYRV
CQILDLPFRQ VSYVKEYWND VFSDFLNEYE KGRTPNPDII CNKHIKFSCF FRYAVDNLGA
DAIATGHYAR TSQEDGEVFQ QKHIKRPEGL FRNRFEVRNA VKLLQAADSF KDQTFFLSQV
SQDALRRTIF PLGGLTKDFV KKIAAENRLH HVLQKKESMG MCFIGKRNFE HFLLQYLPSR
PGQFISIEDH KVLGTHKGWF LYTLGQRANI GGLRAPWYVV EKDSAKGDVF VAPRLDHPAL
YRDLLRTSRV HWITEEPPAA LVRDKMMECH FRFRHQMALV PCVLTLNQDG TVWVTAVQAV
HALATGQFAV FYKGGECLGS GKILRLGPSA YTLQKGQRQA GVPTESPSDS PEEGPDLRPS
L
//
