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Database: UniProt
Entry: A6QAL0
LinkDB: A6QAL0
Original site: A6QAL0 
ID   MNME_SULNB              Reviewed;         450 AA.
AC   A6QAL0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   07-JUN-2017, entry version 74.
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=SUN_1569;
OS   Sulfurovum sp. (strain NBC37-1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Sulfurovum.
OX   NCBI_TaxID=387093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBC37-1;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009179; BAF72519.1; -; Genomic_DNA.
DR   ProteinModelPortal; A6QAL0; -.
DR   SMR; A6QAL0; -.
DR   STRING; 387093.SUN_1569; -.
DR   EnsemblBacteria; BAF72519; BAF72519; SUN_1569.
DR   KEGG; sun:SUN_1569; -.
DR   eggNOG; ENOG4105C1H; Bacteria.
DR   eggNOG; COG0486; LUCA.
DR   HOGENOM; HOG000200713; -.
DR   KO; K03650; -.
DR   OMA; CEIQCHG; -.
DR   OrthoDB; POG091H01GD; -.
DR   Proteomes; UP000006378; 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   PRINTS; PR00326; GTP1OBG.
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;
KW   Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Potassium; Reference proteome;
KW   tRNA processing.
FT   CHAIN         1    450       tRNA modification GTPase MnmE.
FT                                /FTId=PRO_0000345913.
FT   DOMAIN      218    377       TrmE-type G.
FT   NP_BIND     228    233       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   NP_BIND     247    253       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   NP_BIND     272    275       GTP. {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   METAL       228    228       Potassium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   METAL       232    232       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   METAL       247    247       Potassium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   METAL       249    249       Potassium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   METAL       252    252       Potassium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   METAL       253    253       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00379}.
FT   BINDING      25     25       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   BINDING      83     83       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   BINDING     122    122       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
FT   BINDING     450    450       Formyltetrahydrofolate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00379}.
SQ   SEQUENCE   450 AA;  49943 MW;  0D844516983721FC CRC64;
     MEKKMQNTIA AIATAYGVSS ISIIRVSGNA ALDIAKKISH LEEVKPRHAH LTSLYNSQND
     LIDQAIMIYF KAPFSFTGEE IVEFQCHGGM IVAQEILDTI LSYGIRLAEP GEFSKRAFFN
     GKIDLTEAEA ISKLIEAKSV DAAKILAKQM KGELKYFVDE SRDALLRSLA YSEVMIDYAE
     EDIPDDIMRS IVTQLDGLSE QIMKIVDASY RRRGLIEGFK VAIIGKPNVG KSSLLNALLS
     YDRAIVSDIA GTTRDTIEEQ VRIGSHIIRL VDTAGIRESE DTIEKIGIER SLSSVEDADI
     IIALFDGSRE FDSEDEKILA IVDALQDKHI IVAINKSDLE MKLDGDRINS YDPIEVSAKK
     GFVKLTRQME ALLDSIGEGE ELMLISARQI EAVNRAKNAI AEAKEPLMNG ELEFFSYHLQ
     EAVKAISSIS KPYDSEEILD KMFGEFCLGK
//
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