ID C9LV31_SELS3 Unreviewed; 459 AA.
AC C9LV31;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
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:EEX77265.1};
GN Synonyms=mnmE {ECO:0000256|HAMAP-Rule:MF_00379};
GN OrderedLocusNames=Selsp_2293 {ECO:0000313|EMBL:AEC01237.1};
GN ORFNames=SELSPUOL_01321 {ECO:0000313|EMBL:EEX77265.1};
OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=546271 {ECO:0000313|EMBL:EEX77265.1, ECO:0000313|Proteomes:UP000003505};
RN [1] {ECO:0000313|EMBL:EEX77265.1, ECO:0000313|Proteomes:UP000003505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:EEX77265.1}, and ATCC 35185 / DSM
RC 20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000003505};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEC01237.1, ECO:0000313|Proteomes:UP000011124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35185 {ECO:0000313|EMBL:AEC01237.1}, and ATCC 35185 / DSM
RC 20758 / VPI D19B-28 {ECO:0000313|Proteomes:UP000011124};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Selenomonas sputigena DSM 20758.";
RL Submitted (APR-2011) 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; CP002637; AEC01237.1; -; Genomic_DNA.
DR EMBL; ACKP02000023; EEX77265.1; -; Genomic_DNA.
DR RefSeq; WP_006192622.1; NZ_GG698597.1.
DR AlphaFoldDB; C9LV31; -.
DR STRING; 546271.Selsp_2293; -.
DR KEGG; ssg:Selsp_2293; -.
DR eggNOG; COG0486; Bacteria.
DR HOGENOM; CLU_019624_4_1_9; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000003505; Unassembled WGS sequence.
DR Proteomes; UP000011124; 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 PRINTS; PR00326; GTP1OBG.
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|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:UP000011124};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00379}.
FT DOMAIN 222..380
FT /note="TrmE-type G"
FT /evidence="ECO:0000259|PROSITE:PS51709"
FT BINDING 23
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 459
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 459 AA; 49392 MW; 1C5A0E58E4C677A0 CRC64;
MQQADTISAI ATAVGEGGVG IVRLSGASAI ETASRMFCAA GARKLADAGA RDLLYGTVVR
EDGRLVDEAL CLVMRAPHSY TKEDVVELQC HGGAVSLREV LALTYRHGAR AAERGEFTKR
AFLNGRLDLA EAQAVMDVVQ AKTEKGLEMA AGHLAGHFSE RIRSMREDIL ALLAHLEAVI
DFPEEGVDEI VVEEAREKVS ALHASLRRIV QTAHTGRILR DGLETAIVGR PNVGKSSLLN
ALLREDRAIV TDVPGTTRDT IEEYADIGGV PLRIIDTAGI RTTEDAVERI GVEKARAHVK
SAALVLALFD GSRPLEAEDE EILALLEGKD ALIVVTKSDL PRVLDTERLQ NLVHLPLIEI
TTKEEEGISP LAAAILEKVY DGEERSGEGS FVADLRTKNL LEAAADHLTA AISTMDQGLG
LDFISIDLRS SLEKLGEITG ETVGDDVLDE IFSRFCVGK
//
