Tag | Content |
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CPLM ID | CPLM-013502 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | tRNA pseudouridine synthase D |
Protein Synonyms/Alias | tRNA pseudouridine(13) synthase; tRNA pseudouridylate synthase D; tRNA-uridine isomerase D |
Gene Name | truD |
Gene Synonyms/Alias | ygbO; b2745; JW2715 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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64 | FVADALAKFLKIHAR | acetylation | [1] | 81 | SFAGQKDKHAVTEQW | acetylation | [1] | 293 | QALLVREKVEAARRA | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Responsible for synthesis of pseudouridine from uracil- 13 in transfer RNAs. |
Sequence Annotation | DOMAIN 155 303 TRUD. REGION 180 187 RNA binding (Probable). ACT_SITE 31 31 Proton acceptor (Potential). ACT_SITE 80 80 Nucleophile. BINDING 27 27 Substrate (By similarity). BINDING 129 129 Substrate (Probable). BINDING 329 329 Substrate (By similarity). |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Isomerase; Reference proteome; tRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 349 AA |
Protein Sequence | MIEFDNLTYL HGKPQGTGLL KANPEDFVVV EDLGFEPDGE GEHILVRILK NGCNTRFVAD 60 ALAKFLKIHA REVSFAGQKD KHAVTEQWLC ARVPGKEMPD LSAFQLEGCQ VLEYARHKRK 120 LRLGALKGNA FTLVLREVSN RDDVEQRLID ICVKGVPNYF GAQRFGIGGS NLQGAQRWAQ 180 TNTPVRDRNK RSFWLSAARS ALFNQIVAER LKKADVNQVV DGDALQLAGR GSWFVATTEE 240 LAELQRRVND KELMITAALP GSGEWGTQRE ALAFEQAAVA AETELQALLV REKVEAARRA 300 MLLYPQQLSW NWWDDVTVEI RFWLPAGSFA TSVVRELINT TGDYAHIAE 349 |
Gene Ontology | GO:0009982; F:pseudouridine synthase activity; IEA:HAMAP. GO:0003723; F:RNA binding; IEA:InterPro. GO:0031119; P:tRNA pseudouridine synthesis; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |