SPM_002455
  | Uniprot: A0A037UQS9
Description: tRNA modification GTPase TrmE EC number: 3.6.-.- Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: Cofactor: COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-Rule:MF_00379}; ; Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00379} Enzyme regulation: Function [CC]: FUNCTION: 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. {ECO:0000256|HAMAP-Rule:MF_00379}. Pathway: Active site: Binding site: BINDING 22 22 Formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_00379}.; BINDING 80 80 Formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_00379}.; BINDING 119 119 Formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_00379}.; BINDING 449 449 Formyltetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_00379}. Calcium binding: DNA binding: Metal binding: METAL 226 226 Potassium. {ECO:0000256|HAMAP-Rule:MF_00379}.; METAL 230 230 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00379}.; METAL 245 245 Potassium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_00379}.; METAL 247 247 Potassium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_00379}.; METAL 250 250 Potassium. {ECO:0000256|HAMAP-Rule:MF_00379}.; METAL 251 251 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00379}. Nucleotide binding: NP_BIND 226 231 GTP. {ECO:0000256|HAMAP-Rule:MF_00379}.; NP_BIND 245 251 GTP. {ECO:0000256|HAMAP-Rule:MF_00379}.; NP_BIND 270 273 GTP. {ECO:0000256|HAMAP-Rule:MF_00379}. Site: Gene names (primary): mnmE Gene names (synonym): trmE Mass: 50,091 Subunit structure [CC]: SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits. {ECO:0000256|HAMAP-Rule:MF_00379}. Gene ontology (GO): cytoplasm [GO:0005737]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; tRNA modification [GO:0006400] Gene ontology IDs: GO:0003924; GO:0005525; GO:0005737; GO:0006400; GO:0046872 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family. {ECO:0000256|HAMAP-Rule:MF_00379, ECO:0000256|RuleBase:RU003313, ECO:0000256|SAAS:SAAS00534589}.; SIMILARITY: Contains TrmE-type G (guanine nucleotide-binding) domain. {ECO:0000256|SAAS:SAAS00027953}. Protein families: TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, TrmE GTPase family Coiled coil: Domain [FT]: DOMAIN 216 370 TrmE-type G (guanine nucleotide-binding). {ECO:0000259|PROSITE:PS51709}. Motif: Region: EMBL: AGBZ02000001 ProteinModelPortal: A0A037UQS9 MEROPS: EnsemblBacteria KO: KAI92876 UniPathway: CDD: Gene3D: HAMAP: 1.20.120.430;3.30.1360.120;3.40.50.300 InterPro: MF_00379 PANTHER: IPR031168;IPR018948;IPR006073;IPR004520;IPR027368;IPR025867;IPR027417;IPR005225;IPR027266 PIRSF: PRINTS: PROSITE: Pfam: PS51709 ProDom: PF01926;PF12631;PF10396 SMART: SUPFAM: TIGRFAMs: SSF52540 |
455612-456962(-) >nucleotide sequence ACCTAGAATATCACCCAATATTTCTCAAGCCTCATGTAAGTCGACATTAATAATATCAAC CGGAAATCCACTCGTACTATTATTATATGCATTTTTTATTGAATTTGCTACCTTCTCTAA TAAAGAAATTTGTTTTATATTTGATAAAACTAGTTGATCATCTTTTGTAATTTGTGCCGT TTTATATAAATTTAAAATTTTATCAATAAGAGACTTGATATCTCGCTTTAATGCTGAAAT CAAAAGAATATTTTGCTGTAAATTTTTCTTTTGTGTTTGCATATTAAGTAAATCGGTTTT ATTTAACACTAACAAATATTCTTTATTTTTAATCAGTTCTTTAAGCTCCGGATTTAAATT AATTAAATCAGCATAATTATCAGCGACAATTAAAATTAAATCAGCATTAATAACTTGTTG ACGTGCTTTATCAATTCCAATTTGCTCAATTTTATCAACTGTCTCACGTAAACCAGCTGT ATCAATAATATTTAGGGTTAATGGTCCTAAATTAATCTTCCCTTCAACAATATCTCTTGT TGTTCCTGGCAAGTCAGAAACAATAGCTTTATCTTCGTTCATTAATGCATTTAATAATGA TGACTTTCCAACATTTGGTTTTCCTAAAATTAAGACATTAATACCATCATCGATCATTTT CCCAACTTTACTAATTTTAACTAAATCATTAATTTTTTGTTCTAAAATTAATAAACGCTG ATTTAATTCTTGTGTAGTTAAATCACCAACACCATCATATTCAGGGTAATCAATATTTAC TTCAATATTTGCAATAATATCTAACAGTTCATCACGATAAGTACTAATTAAATAAGTATT TTTATTTTGTAAATTATTTAAAGCTATTTTTGCACTAGTGTCATTTGTTGCATTAACTAA GTTATTAATAGCATCTGTTTGAATTAAATTAAGTTTTCCATTTAAAAATGCTCGTTGCGA AAATTCACCTTTATTTGCTAAACGTGCACCATTTTTTAGTAATAACTTAATAATATTATT TGTAACTAATACACCACCATGACAATTAATTTCAATAATGTCTTCTCCCGTAAAAGAATT AGGTTTTTGAAAACAAACTAAAATAACTTGGTCAATAATCTCTTTACCATCTCGTAAATA ACCATAGTAAATTTGATTCCCCTCTTGAATAATTTTTTTTGAAAAAACTTTATTAATAAT TTTATAACTATCTACCCCAGACATGCGAATAATTGCAATTGCTTGTTTTACCATTGCAGT TGCTGGGGCAATTATTGTATCTTCAATCAT >protein sequence QVILVCFQKPNSFTGEDIIEINCHGGVLVTNNIIKLLLKNGARLANKGEFSQRAFLNGKL NLIQTDAINNLVNATNDTSAKIALNNLQNKNTYLISTYRDELLDIIANIEVNIDYPEYDG VGDLTTQELNQRLLILEQKINDLVKISKVGKMIDDGINVLILGKPNVGKSSLLNALMNED KAIVSDLPGTTRDIVEGKINLGPLTLNIIDTAGLRETVDKIEQIGIDKARQQVINADLIL IVADNYADLINLNPELKELIKNKEYLLVLNKTDLLNMQTQKKNLQQNILLISALKRDIKS LIDKILNLYKTAQITKDDQLVLSNIKQISLLEKVANSIKNAYNNSTSGFPVDIINVDLHE AWEILGDILGENYEEDLLTTIFSKYCLGK |
© Fisunov Lab of Proteomics, 2016.