(data stored in ACNUC7421 zone)

SWISSPROT: MNME_RHOPS

ID   MNME_RHOPS              Reviewed;         460 AA.
AC   Q13E22;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   11-DEC-2019, entry version 84.
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=RPD_0429;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
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., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-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) group at
CC       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 subunits.
CC       {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-like
CC       GTPase superfamily. TrmE GTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00379}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE37667.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000283; ABE37667.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041805583.1; NC_007958.1.
DR   SMR; Q13E22; -.
DR   STRING; 316057.RPD_0429; -.
DR   PRIDE; Q13E22; -.
DR   EnsemblBacteria; ABE37667; ABE37667; RPD_0429.
DR   KEGG; rpd:RPD_0429; -.
DR   eggNOG; ENOG4105C1H; Bacteria.
DR   eggNOG; COG0486; LUCA.
DR   HOGENOM; HOG000200714; -.
DR   KO; K03650; -.
DR   OrthoDB; 263682at2; -.
DR   BioCyc; RPAL316057:RPD_RS02205-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 1.
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; Q13E22.
DR   SWISS-2DPAGE; Q13E22.
KW   Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Potassium; tRNA processing.
FT   CHAIN           1..460
FT                   /note="tRNA modification GTPase MnmE"
FT                   /id="PRO_0000345893"
FT   DOMAIN          218..385
FT                   /note="TrmE-type G"
FT   NP_BIND         228..233
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   NP_BIND         247..253
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   NP_BIND         272..275
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   METAL           232
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   METAL           253
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         24
FT                   /note="Formyltetrahydrofolate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         81
FT                   /note="Formyltetrahydrofolate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         121
FT                   /note="Formyltetrahydrofolate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         460
FT                   /note="Formyltetrahydrofolate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
SQ   SEQUENCE   460 AA;  48819 MW;  9B1245B9FD84D661 CRC64;
     MHPSDQTIFA LATGQLPSAI AMVRVSGPRA GDLLTALTGS LPPPRTARRV LIRDQNQDLI
     DDGVALWFAG PASATGEDVA EFHIHGGRAV LAALVRALSA FDGVRPAEPG EFTRRAFENG
     KLDLTEAEGL DDLIHADTEA QRRQAVRQLG GLLGDRARRW RAQIIEATAL IEAGIDFADE
     GDVQGELMAP ALQTIAALHD EIAEVLAAQG RSERLRDGMV VAIAGPPNVG KSTLINRLAR
     REVAIVSPHA GTTRDVIEVQ LDLGGYPVTV IDTAGIRESN DPVEQEGVRR ARARAAEADL
     VLWLGEGEMT GDAVAASAPV WRVRNKIDLR GGEGDGGPVG LPVEPLAAAL RQTDGAWGGN
     AAFEISALRG QGLGELIAAI EDFAAQYFAS GETALISRAR HRTLLQDAAA MLQRSLQHDL
     PAELVAEELR LAGVALGRLL GRVDVEDVLG EIFSRFCIGK
//

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