CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005409
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 tRNA modification GTPase MnmE 
Protein Synonyms/Alias
  
Gene Name
 mnmE 
Gene Synonyms/Alias
 thdF; trmE; b3706; JW3684 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
327FIARLPAKLPITVVRacetylation[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
 Exhibits a very high intrinsic GTPase hydrolysis rate. 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
 DOMAIN 218 336 G.
 NP_BIND 226 231 GTP.
 NP_BIND 245 251 GTP.
 NP_BIND 270 273 GTP.
 NP_BIND 335 338 GTP.
 NP_BIND 358 360 GTP.
 METAL 226 226 Potassium.
 METAL 230 230 Magnesium.
 METAL 245 245 Potassium; via carbonyl oxygen.
 METAL 247 247 Potassium; via carbonyl oxygen.
 METAL 250 250 Potassium.
 METAL 251 251 Magnesium.
 BINDING 23 23 Formyltetrahydrofolate (By similarity).
 BINDING 80 80 Formyltetrahydrofolate (By similarity).
 BINDING 120 120 Formyltetrahydrofolate (By similarity).
 BINDING 454 454 Formyltetrahydrofolate (By similarity).  
Keyword
 3D-structure; Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding; Potassium; Reference proteome; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 454 AA 
Protein Sequence
MSDNDTIVAQ ATPPGRGGVG ILRISGFKAR EVAETVLGKL PKPRYADYLP FKDADGSVLD 60
QGIALWFPGP NSFTGEDVLE LQGHGGPVIL DLLLKRILTI PGLRIARPGE FSERAFLNDK 120
LDLAQAEAIA DLIDASSEQA ARSALNSLQG AFSARVNHLV EALTHLRIYV EAAIDFPDEE 180
IDFLSDGKIE AQLNDVIADL DAVRAEARQG SLLREGMKVV IAGRPNAGKS SLLNALAGRE 240
AAIVTDIAGT TRDVLREHIH IDGMPLHIID TAGLREASDE VERIGIERAW QEIEQADRVL 300
FMVDGTTTDA VDPAEIWPEF IARLPAKLPI TVVRNKADIT GETLGMSEVN GHALIRLSAR 360
TGEGVDVLRN HLKQSMGFDT NMEGGFLARR RHLQALEQAA EHLQQGKAQL LGAWAGELLA 420
EELRLAQQNL SEITGEFTSD DLLGRIFSSF CIGK 454 
Gene Ontology
 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0005525; F:GTP binding; IDA:EcoCyc.
 GO:0003924; F:GTPase activity; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0009268; P:response to pH; IMP:EcoCyc.
 GO:0030488; P:tRNA methylation; IMP:EcoCyc.
 GO:0006805; P:xenobiotic metabolic process; IMP:EcoCyc. 
Interpro
 IPR018948; GTP-bd_TrmE_N.
 IPR006073; GTP_binding_domain.
 IPR004520; GTPase_MnmE.
 IPR025867; GTPase_MnmE_C_dom.
 IPR027368; MnmE_dom2.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR027266; TrmE/GcvT_dom1. 
Pfam
 PF12631; GTPase_Cys_C
 PF01926; MMR_HSR1
 PF10396; TrmE_N 
SMART
  
PROSITE
  
PRINTS