ID A0A1M6IYX0_9CLOT Unreviewed; 460 AA.
AC A0A1M6IYX0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=mnmE {ECO:0000256|HAMAP-Rule:MF_00379};
GN Synonyms=trmE {ECO:0000256|HAMAP-Rule:MF_00379};
GN ORFNames=SAMN02745975_01994 {ECO:0000313|EMBL:SHJ39590.1};
OS Geosporobacter subterraneus DSM 17957.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Geosporobacter.
OX NCBI_TaxID=1121919 {ECO:0000313|EMBL:SHJ39590.1, ECO:0000313|Proteomes:UP000184536};
RN [1] {ECO:0000313|EMBL:SHJ39590.1, ECO:0000313|Proteomes:UP000184536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17957 {ECO:0000313|EMBL:SHJ39590.1,
RC ECO:0000313|Proteomes:UP000184536};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQZV01000023; SHJ39590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6IYX0; -.
DR STRING; 1121919.SAMN02745975_01994; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000184536; Unassembled WGS sequence.
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; SSF103025; Folate-binding domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF116878; TrmE connector domain; 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|ARBA:ARBA00022842, 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 tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00379}.
FT DOMAIN 222..381
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 87
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 126
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 232..237
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 232
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 251..257
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 251
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 253
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 256
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 276..279
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 460
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 460 AA; 50876 MW; 5673091346E176E8 CRC64;
MIDDTIAAIG TAPGEAGIGI VRMSGPDAVS ILDKLFVPTR GNSILEYGGR RLTHGHIVDP
DTKNRVDEVL VTYMKAPYTY TAEDVTEIDC HGGIVPVRKI LELVLRHGAR IAEPGEFTKR
AFLNGRIDLA QAEAVMDLIR AKTDVGFDVA LGQLEGSLSK EVKRIRDKLL EMLAHITVNI
DFPDEDIEEI TYRTLKEQAE EIIGDIEGLL KTAHTGKIIR EGLSTVIIGK PNVGKSSLMN
ALLRESRAIV TDIPGTTRDV IEEYVNIQGI PLRIIDTAGI RETEDFIEKI GVERSKEFFN
RADLIIFVLN AAEPLSSEDE QIMKLVEHRD AIVLINKIDL PAKLEESKIQ ELLPGKRIIP
ISVLEGKGLQ ELEEAIVKMV YGGEVKHQDH SFVTNARHKN ALERSKKSME DAVGAIGQGM
PLDFIEVDVK NTWEYLGEIT GDTVGEDLID KIFANFCLGK
//
