ID A0A0H3XJL0_9MOLU Unreviewed; 448 AA.
AC A0A0H3XJL0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=tRNA modification GTPase MnmE {ECO:0000256|HAMAP-Rule:MF_00379};
DE EC=3.6.-.- {ECO:0000256|HAMAP-Rule:MF_00379};
GN Name=trmE {ECO:0000256|HAMAP-Rule:MF_00379,
GN ECO:0000313|EMBL:AKM54780.1};
GN Synonyms=mnmE {ECO:0000256|HAMAP-Rule:MF_00379};
GN ORFNames=SERIO_v1c12310 {ECO:0000313|EMBL:AKM54780.1};
OS Spiroplasma eriocheiris.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=315358 {ECO:0000313|EMBL:AKM54780.1, ECO:0000313|Proteomes:UP000035661};
RN [1] {ECO:0000313|EMBL:AKM54780.1, ECO:0000313|Proteomes:UP000035661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDA-040725-5 {ECO:0000313|Proteomes:UP000035661};
RX PubMed=26254485; DOI=10.1093/gbe/evv160;
RA Lo W.S., Gasparich G.E., Kuo C.H.;
RT "Found and Lost: The Fates of Horizontally Acquired Genes in Arthropod-
RT Symbiotic Spiroplasma.";
RL Genome Biol. Evol. 7:2458-2472(2015).
RN [2] {ECO:0000313|Proteomes:UP000035661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDA-040725-5 {ECO:0000313|Proteomes:UP000035661};
RA Lo W.-S., Kuo C.-H.;
RT "Complete genome sequence of Spiroplasma eriocheiris TDA-040725-5 (DSM
RT 21848).";
RL Submitted (JUN-2015) 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:0000256|HAMAP-Rule:MF_00379}.
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00379};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00379};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00379}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00379}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. TrmE GTPase family. {ECO:0000256|ARBA:ARBA00011043,
CC ECO:0000256|HAMAP-Rule:MF_00379, ECO:0000256|RuleBase:RU003313}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00379}.
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DR EMBL; CP011856; AKM54780.1; -; Genomic_DNA.
DR RefSeq; WP_047791955.1; NZ_CP011856.1.
DR AlphaFoldDB; A0A0H3XJL0; -.
DR STRING; 315358.SERIO_v1c12310; -.
DR KEGG; seri:SERIO_v1c12310; -.
DR PATRIC; fig|743698.3.peg.1243; -.
DR Proteomes; UP000035661; 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 CDD; cd14858; TrmE_N; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.430; tRNA modification GTPase MnmE domain 2; 1.
DR HAMAP; MF_00379; GTPase_MnmE; 1.
DR InterPro; IPR031168; G_TrmE.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR018948; GTP-bd_TrmE_N.
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 NCBIfam; TIGR00450; mnmE_trmE_thdF; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42714; TRNA MODIFICATION GTPASE GTPBP3; 1.
DR PANTHER; PTHR42714:SF2; TRNA MODIFICATION GTPASE GTPBP3, MITOCHONDRIAL; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF12631; MnmE_helical; 1.
DR Pfam; PF10396; TrmE_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51709; G_TRME; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00379};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00379}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00379};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00379};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00379};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00379};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00379};
KW Reference proteome {ECO:0000313|Proteomes:UP000035661};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00379}.
FT DOMAIN 216..369
FT /note="TrmE-type G"
FT /evidence="ECO:0000259|PROSITE:PS51709"
FT BINDING 22
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 80
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 119
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 226..231
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 245..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 448
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
SQ SEQUENCE 448 AA; 49864 MW; 59BD69500EA66429 CRC64;
MINDTIVAPT TSMMNQAISI IRLSGPDAFP IINKIFSKVV KPHKNEIHYG FIKDGAETLD
QVLLMCFENP NSFTGEDVIE INCHGGVYIT NKILKLLLKN GARLANRGEF SQRAFLNGKI
NLIQAEAIND LVHATNDQSA KIAISNLQNK NISVINNFRN DLLDIIANIE VNIDYPEYDG
VGNLTVGELH EKLKVLSNRI AEIIALSKIG KVINDGVNLV ILGQPNVGKS SLLNALLNED
KAIVSDTPGT TRDIVEGRVN IGNLTLNLID TAGIRTTDNE IERIGINKAK EQITLADLVL
LVFDSTRSLS VEEQELLELT KNKKRIIIIN KIDLNPHHQY RFSADHQIEM AAINRDIKSL
INKINELFST DQLFKDDTII LSNIKQISIL ENVEKSLKNA YNNSTDGFPV DIVNVDLHES
WNLLGELLGE SYDDNLLDTM FSKYCLGK
//
