(data stored in ACNUC7421 zone)

SWISSPROT: MNME_PARDP

ID   MNME_PARDP              Reviewed;         419 AA.
AC   A1AXX6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=Pden_0003;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) 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; CP000489; ABL68120.1; -; Genomic_DNA.
DR   RefSeq; WP_011746353.1; NC_008686.1.
DR   SMR; A1AXX6; -.
DR   STRING; 318586.Pden_0003; -.
DR   PRIDE; A1AXX6; -.
DR   EnsemblBacteria; ABL68120; ABL68120; Pden_0003.
DR   KEGG; pde:Pden_0003; -.
DR   eggNOG; ENOG4105C1H; Bacteria.
DR   eggNOG; COG0486; LUCA.
DR   HOGENOM; HOG000200714; -.
DR   KO; K03650; -.
DR   OMA; CEIQCHG; -.
DR   BioCyc; PDEN318586:G1GW1-3-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd04164; trmE; 1.
DR   Gene3D; 1.20.120.430; -; 1.
DR   Gene3D; 3.30.1360.120; -; 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; IPR027368; MnmE_dom2.
DR   InterPro; IPR025867; MnmE_helical.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF12631; MnmE_helical; 1.
DR   Pfam; PF10396; TrmE_N; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
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; A1AXX6.
DR   SWISS-2DPAGE; A1AXX6.
KW   Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Potassium; Reference proteome;
KW   tRNA processing.
FT   CHAIN         1    419       tRNA modification GTPase MnmE.
FT                                /FTId=PRO_0000345861.
FT   DOMAIN      211    348       TrmE-type G.
FT   NP_BIND     221    226       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   NP_BIND     240    246       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   NP_BIND     265    268       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   METAL       221    221       Potassium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   METAL       225    225       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   METAL       240    240       Potassium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   METAL       242    242       Potassium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   METAL       245    245       Potassium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   METAL       246    246       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   BINDING      20     20       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   BINDING      76     76       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   BINDING     115    115       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   BINDING     419    419       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
SQ   SEQUENCE   419 AA;  44695 MW;  3F2A6293507E85FF CRC64;
     MDTIFAEATP PGRGGVSVVR LSGPKAHATL ESLAGPVATP RMAALRALRD GDDLIDRALV
     IWFAEGHSFT GEEVAELHLH GAPVIASRLS QALLARGLRR AEAGEFTKRA FLNGRIDLAE
     AEGLADLLSA ETEAQRKLAM RATEGELGRK ADELRSKLIR AGALIEASID FADEEVPDEV
     PEEALDLIKA VRSDIQGMLA SYPATERLRQ GYEVAIIGPP NAGKSTLLNR IGQREIALVS
     EIAGTTRDIL ELHTDLRGLP VTFLDTAGLR ESSDPVEAMG VARAVQRAAE ADLRIHLSVD
     GVPEETLVLG DIIVRSKADL GRGEETAISG LTGEGVAELL DLVYDRLRVR AADSGLVGHK
     RQAEALQRAV AALAIDDSLA PEFLAEALRQ AAQALAMMVG RVGAEDYLDE IFSSFCIGK
//

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