Tag | Content |
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CPLM ID | CPLM-009201 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | tRNA pseudouridine synthase B |
Protein Synonyms/Alias | Protein p35; tRNA pseudouridine(55) synthase; Psi55 synthase; tRNA pseudouridylate synthase; tRNA-uridine isomerase |
Gene Name | truB |
Gene Synonyms/Alias | yhbA; b3166; JW3135 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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31 | SSNDALQKVKRIYNA | acetylation | [1] | 74 | QYLLDSDKRYRVIAR | acetylation | [1] | 190 | IIDDLGEKLGCGAHV | acetylation | [1] | 207 | LRRLAVSKYPVERMV | 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- 55 in the psi GC loop of transfer RNAs. |
Sequence Annotation | REGION 124 152 RNA binding (By similarity). ACT_SITE 48 48 Nucleophile. BINDING 43 43 Substrate. BINDING 76 76 Substrate. BINDING 179 179 Substrate (Probable). BINDING 202 202 Substrate. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Isomerase; Reference proteome; tRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 314 AA |
Protein Sequence | MSRPRRRGRD INGVLLLDKP QGMSSNDALQ KVKRIYNANR AGHTGALDPL ATGMLPICLG 60 EATKFSQYLL DSDKRYRVIA RLGQRTDTSD ADGQIVEERP VTFSAEQLAA ALDTFRGDIE 120 QIPSMYSALK YQGKKLYEYA RQGIEVPREA RPITVYELLF IRHEGNELEL EIHCSKGTYI 180 RTIIDDLGEK LGCGAHVIYL RRLAVSKYPV ERMVTLEHLR ELVEQAEQQD IPAAELLDPL 240 LMPMDSPASD YPVVNLPLTS SVYFKNGNPV RTSGAPLEGL VRVTEGENGK FIGMGEIDDE 300 GRVAPRRLVV EYPA 314 |
Gene Ontology | GO:0009982; F:pseudouridine synthase activity; IMP:EcoCyc. GO:0003723; F:RNA binding; IEA:InterPro. GO:0001522; P:pseudouridine synthesis; IDA:EcoCyc. GO:0031119; P:tRNA pseudouridine synthesis; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |