CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020907
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Mitochondrial tRNA-specific 2-thiouridylase 1 
Protein Synonyms/Alias
  
Gene Name
 Trmu 
Gene Synonyms/Alias
 Mtu1; Trmt1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
106INCNKHIKFSCFYHYacetylation[1, 2]
Reference
 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
Functional Description
 Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2- thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base (By similarity). 
Sequence Annotation
 NP_BIND 10 17 ATP (By similarity).
 REGION 96 98 Interaction with target base in tRNA (By
 REGION 171 173 Interaction with tRNA (By similarity).
 REGION 334 335 Interaction with tRNA (By similarity).
 ACT_SITE 101 101 Nucleophile (By similarity).
 ACT_SITE 222 222 Cysteine persulfide intermediate (By
 BINDING 36 36 ATP; via amide nitrogen and carbonyl
 BINDING 126 126 ATP; via amide nitrogen (By similarity).
 DISULFID 101 222 Alternate (By similarity).  
Keyword
 ATP-binding; Complete proteome; Disulfide bond; Mitochondrion; Nucleotide-binding; Reference proteome; RNA-binding; Transferase; tRNA processing; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 417 AA 
Protein Sequence
MSALRHVVCA LSGGVDSAVA ALLLRRRGYQ VTGVFMKNWD SLDEQGVCAA DKDCEDAYKV 60
CQILDIPFHQ VSYVKEYWND VFSDFLNEYE KGRTPNPDIN CNKHIKFSCF YHYAVDNLGA 120
DAVATGHYAR TSLEDEEVFE QKHTKKPDGL FRNRFEVRNP VKLLQAADSF KDQTFFLSQV 180
SQDALRRTIF PLGELTKDFV KKIAAENSLH HVLQKRESMG ICFIGKRNLE HFLLQYLQPR 240
PGKFVSIEDN TVLGTHKGWF LYTLGQRAKI SGLREPWYVV EKDGTKGDVL VAPRVDHPAL 300
YRDLLRTNRV HWIAEEPPAA LVRDKMMECH FRFRHQMALV PCVLTLNQDG TVWVTAVKAV 360
RGLALGQFAV FYKGEECLGS GKILRLGPSA YTLQKGKNRT RVAPEASSDS PGLHPTS 417 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. 
Interpro
 IPR023382; Adenine_a_hdrlase_dom.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR004506; tRNA-specific_2-thiouridylase. 
Pfam
 PF03054; tRNA_Me_trans 
SMART
  
PROSITE
  
PRINTS