(data stored in ACNUC7421 zone)

SWISSPROT: MNME_SHESH

ID   MNME_SHESH              Reviewed;         453 AA.
AC   A8FP41;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 69.
DE   RecName: Full=tRNA modification GTPase MnmE {ECO:0000255|HAMAP-Rule:MF_00379};
DE            EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_00379};
GN   Name=mnmE {ECO:0000255|HAMAP-Rule:MF_00379};
GN   Synonyms=trmE {ECO:0000255|HAMAP-Rule:MF_00379};
GN   OrderedLocusNames=Ssed_0001;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exhibits a very high intrinsic GTPase hydrolysis rate.
CC       Involved in the addition of a carboxymethylaminomethyl (cmnm)
CC       group at the wobble position (U34) of certain tRNAs, forming tRNA-
CC       cmnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_00379}.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00379};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00379};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00379}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00379}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
CC       like GTPase superfamily. TrmE GTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00379}.
DR   EMBL; CP000821; ABV34614.1; -; Genomic_DNA.
DR   RefSeq; WP_012004141.1; NC_009831.1.
DR   ProteinModelPortal; A8FP41; -.
DR   SMR; A8FP41; -.
DR   STRING; 425104.Ssed_0001; -.
DR   EnsemblBacteria; ABV34614; ABV34614; Ssed_0001.
DR   KEGG; sse:Ssed_0001; -.
DR   eggNOG; ENOG4105C1H; Bacteria.
DR   eggNOG; COG0486; LUCA.
DR   HOGENOM; HOG000200714; -.
DR   KO; K03650; -.
DR   OMA; CEIQCHG; -.
DR   OrthoDB; POG091H01GD; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   CDD; cd04164; trmE; 1.
DR   HAMAP; MF_00379; GTPase_MnmE; 1.
DR   InterPro; IPR031168; G_TrmE.
DR   InterPro; IPR018948; GTP-bd_TrmE_N.
DR   InterPro; IPR006073; GTP_binding_domain.
DR   InterPro; IPR004520; GTPase_MnmE.
DR   InterPro; IPR025867; MnmE_helical.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF12631; MnmE_helical; 1.
DR   Pfam; PF10396; TrmE_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51709; G_TRME; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FP41.
DR   SWISS-2DPAGE; A8FP41.
KW   Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Potassium; tRNA processing.
FT   CHAIN         1    453       tRNA modification GTPase MnmE.
FT                                /FTId=PRO_1000080016.
FT   DOMAIN      215    376       TrmE-type G.
FT   NP_BIND     225    230       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   NP_BIND     244    250       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   NP_BIND     269    272       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   NP_BIND     334    337       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   METAL       225    225       Potassium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   METAL       229    229       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   METAL       244    244       Potassium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   METAL       246    246       Potassium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   METAL       249    249       Potassium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   METAL       250    250       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   BINDING      22     22       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   BINDING      79     79       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   BINDING     119    119       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   BINDING     453    453       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
SQ   SEQUENCE   453 AA;  49259 MW;  70CF2A5BAFC219E8 CRC64;
     MTTDTIVAQA TAPGRGGVGI IRISGDQASE VAMALLGHIP KTRYADYCDF KDGEGEVIDQ
     GIALYFQGPN SFTGEDVLEL QGHGGQIVLD MLIKRVMEVE GIRIAKPGEF SEQAFMNDKL
     DLTQAEAIAD LIDATSEQAA KSALNSLQGE FSTQVHELVD RVTNLRLYVE AAIDFPDEEV
     DFLSDGKIAG SLYRIITKLD SVQASAKQGA IIREGMKVVI AGRPNAGKSS LLNALAGKES
     AIVTEIAGTT RDVLREHIHL DGMPLHIIDT AGLRDTADTV EQIGIERAWA EIETADQVLF
     MVDGTTTDAV DPHEIWPDFI DRLPEKLGIT VVRNKADITG EALTVTQDHG HNVFRISAKT
     GLGVEELQQH LKSLMGYQSN LEGGFIARRR HLEALELATS HLMIGKEQLE VYQAGELLAE
     ELRMTQMALS EITGKFTSDD LLGKIFSSFC IGK
//

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