Tag | Content |
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CPLM ID | CPLM-002941 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG |
Protein Synonyms/Alias | Glucose-inhibited division protein A |
Gene Name | mnmG |
Gene Synonyms/Alias | gidA; trmF; b3741; JW3719 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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145 | AVTQMGLKFRAKAVV | acetylation | [1] | 283 | YCPSIEDKVMRFADR | acetylation | [1] | 398 | AARLSADKEGWAPAR | acetylation | [1] | 589 | LSNEVIAKLNDHKPA | 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 | NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. |
Sequence Annotation | NP_BIND 13 18 FAD (By similarity). NP_BIND 273 287 NAD (Potential). BINDING 125 125 FAD; via amide nitrogen and carbonyl BINDING 180 180 FAD (By similarity). BINDING 370 370 FAD (By similarity). |
Keyword | 3D-structure; Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome; tRNA processing. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 629 AA |
Protein Sequence | MFYPDPFDVI IIGGGHAGTE AAMAAARMGQ QTLLLTHNID TLGQMSCNPA IGGIGKGHLV 60 KEVDALGGLM AKAIDQAGIQ FRILNASKGP AVRATRAQAD RVLYRQAVRT ALENQPNLMI 120 FQQAVEDLIV ENDRVVGAVT QMGLKFRAKA VVLTVGTFLD GKIHIGLDNY SGGRAGDPPS 180 IPLSRRLREL PLRVGRLKTG TPPRIDARTI DFSVLAQQHG DNPMPVFSFM GNASQHPQQV 240 PCYITHTNEK THDVIRSNLD RSPMYAGVIE GVGPRYCPSI EDKVMRFADR NQHQIFLEPE 300 GLTSNEIYPN GISTSLPFDV QMQIVRSMQG MENAKIVRPG YAIEYDFFDP RDLKPTLESK 360 FIQGLFFAGQ INGTTGYEEA AAQGLLAGLN AARLSADKEG WAPARSQAYL GVLVDDLCTL 420 GTKEPYRMFT SRAEYRLMLR EDNADLRLTE IGRELGLVDD ERWARFNEKL ENIERERQRL 480 KSTWVTPSAE AAAEVNAHLT APLSREASGE DLLRRPEMTY EKLTTLTPFA PALTDEQAAE 540 QVEIQVKYEG YIARQQDEIE KQLRNENTLL PATLDYRQVS GLSNEVIAKL NDHKPASIGQ 600 ASRISGVTPA AISILLVWLK KQGMLRRSA 629 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0050660; F:flavin adenine dinucleotide binding; IDA:EcoCyc. GO:0030488; P:tRNA methylation; IMP:EcoCyc. GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |