| Tag | Content |
|---|
| CPLM ID | CPLM-003057 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Queuine tRNA-ribosyltransferase |
Protein Synonyms/Alias | Guanine insertion enzyme; tRNA-guanine transglycosylase |
Gene Name | tgt |
Gene Synonyms/Alias | b0406; JW0396 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 239 | CPQIPADKPRYLMGV | acetylation | [1] | | 248 | RYLMGVGKPEDLVEG | acetylation | [1] | | 285 | FVTDGVVKIRNAKYK | acetylation | [1] | | 353 | RKAIEEGKLESFVTD | acetylation | [1] |
|
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 | Exchanges the guanine residue with 7-aminomethyl-7- deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). |
Sequence Annotation | ACT_SITE 89 89 Nucleophile.
METAL 302 302 Zinc.
METAL 304 304 Zinc.
METAL 307 307 Zinc.
METAL 333 333 Zinc (By similarity).
BINDING 90 90 Substrate. |
Keyword | Complete proteome; Direct protein sequencing; Glycosyltransferase; Metal-binding; Queuosine biosynthesis; Reference proteome; Transferase; tRNA processing; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 375 AA |
Protein Sequence | MKFELDTTDG RARRGRLVFD RGVVETPCFM PVGTYGTVKG MTPEEVEATG AQIILGNTFH 60
LWLRPGQEIM KLHGDLHDFM QWKGPILTDS GGFQVFSLGD IRKITEQGVH FRNPINGDPI 120
FLDPEKSMEI QYDLGSDIVM IFDECTPYPA DWDYAKRSME MSLRWAKRSR ERFDSLGNKN 180
ALFGIIQGSV YEDLRDISVK GLVDIGFDGY AVGGLAVGEP KADMHRILEH VCPQIPADKP 240
RYLMGVGKPE DLVEGVRRGI DMFDCVMPTR NARNGHLFVT DGVVKIRNAK YKSDTGPLDP 300
ECDCYTCRNY SRAYLHHLDR CNEILGARLN TIHNLRYYQR LMAGLRKAIE EGKLESFVTD 360
FYQRQGREVP PLNVD 375 |
Gene Ontology | GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:HAMAP. GO:0008616; P:queuosine biosynthetic process; IEA:HAMAP. |
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SMART | |
PROSITE | |
PRINTS | |