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
CTATTTTCCTAGGCAATACTTACTAAAAATTGTTGTTAATAAGTCTTCTTCATAGTTTTC
ACCTAGAATATCACCCAATATTTCTCAAGCCTCATGTAAGTCGACATTAATAATATCAAC
CGGAAATCCACTCGTACTATTATTATATGCATTTTTTATTGAATTTGCTACCTTCTCTAA
TAAAGAAATTTGTTTTATATTTGATAAAACTAGTTGATCATCTTTTGTAATTTGTGCCGT
TTTATATAAATTTAAAATTTTATCAATAAGAGACTTGATATCTCGCTTTAATGCTGAAAT
CAAAAGAATATTTTGCTGTAAATTTTTCTTTTGTGTTTGCATATTAAGTAAATCGGTTTT
ATTTAACACTAACAAATATTCTTTATTTTTAATCAGTTCTTTAAGCTCCGGATTTAAATT
AATTAAATCAGCATAATTATCAGCGACAATTAAAATTAAATCAGCATTAATAACTTGTTG
ACGTGCTTTATCAATTCCAATTTGCTCAATTTTATCAACTGTCTCACGTAAACCAGCTGT
ATCAATAATATTTAGGGTTAATGGTCCTAAATTAATCTTCCCTTCAACAATATCTCTTGT
TGTTCCTGGCAAGTCAGAAACAATAGCTTTATCTTCGTTCATTAATGCATTTAATAATGA
TGACTTTCCAACATTTGGTTTTCCTAAAATTAAGACATTAATACCATCATCGATCATTTT
CCCAACTTTACTAATTTTAACTAAATCATTAATTTTTTGTTCTAAAATTAATAAACGCTG
ATTTAATTCTTGTGTAGTTAAATCACCAACACCATCATATTCAGGGTAATCAATATTTAC
TTCAATATTTGCAATAATATCTAACAGTTCATCACGATAAGTACTAATTAAATAAGTATT
TTTATTTTGTAAATTATTTAAAGCTATTTTTGCACTAGTGTCATTTGTTGCATTAACTAA
GTTATTAATAGCATCTGTTTGAATTAAATTAAGTTTTCCATTTAAAAATGCTCGTTGCGA
AAATTCACCTTTATTTGCTAAACGTGCACCATTTTTTAGTAATAACTTAATAATATTATT
TGTAACTAATACACCACCATGACAATTAATTTCAATAATGTCTTCTCCCGTAAAAGAATT
AGGTTTTTGAAAACAAACTAAAATAACTTGGTCAATAATCTCTTTACCATCTCGTAAATA
ACCATAGTAAATTTGATTCCCCTCTTGAATAATTTTTTTTGAAAAAACTTTATTAATAAT
TTTATAACTATCTACCCCAGACATGCGAATAATTGCAATTGCTTGTTTTACCATTGCAGT
TGCTGGGGCAATTATTGTATCTTCAATCAT


>protein sequence
MIEDTIIAPATAMVKQAIAIIRMSGVDSYKIINKVFSKKIIQEGNQIYYGYLRDGKEIID
QVILVCFQKPNSFTGEDIIEINCHGGVLVTNNIIKLLLKNGARLANKGEFSQRAFLNGKL
NLIQTDAINNLVNATNDTSAKIALNNLQNKNTYLISTYRDELLDIIANIEVNIDYPEYDG
VGDLTTQELNQRLLILEQKINDLVKISKVGKMIDDGINVLILGKPNVGKSSLLNALMNED
KAIVSDLPGTTRDIVEGKINLGPLTLNIIDTAGLRETVDKIEQIGIDKARQQVINADLIL
IVADNYADLINLNPELKELIKNKEYLLVLNKTDLLNMQTQKKNLQQNILLISALKRDIKS
LIDKILNLYKTAQITKDDQLVLSNIKQISLLEKVANSIKNAYNNSTSGFPVDIINVDLHE
AWEILGDILGENYEEDLLTTIFSKYCLGK






















© Fisunov Lab of Proteomics, 2016.