ID A0A1Y2PIJ4_9FLAO Unreviewed; 464 AA.
AC A0A1Y2PIJ4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-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=WH52_02470 {ECO:0000313|EMBL:OSY89518.1};
OS Tenacibaculum holothuriorum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1635173 {ECO:0000313|EMBL:OSY89518.1, ECO:0000313|Proteomes:UP000194221};
RN [1] {ECO:0000313|EMBL:OSY89518.1, ECO:0000313|Proteomes:UP000194221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2-2 {ECO:0000313|EMBL:OSY89518.1,
RC ECO:0000313|Proteomes:UP000194221};
RA Shao Z., Wang L., Li X.;
RT "Genome sequence of Tenacibaculum sp. S2-2, isolated from intestinal
RT microbiota of sea cucumber, Apostichopus japonicas.";
RL Submitted (MAR-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OSY89518.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAPZ01000001; OSY89518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2PIJ4; -.
DR STRING; 1635173.WH52_02470; -.
DR InParanoid; A0A1Y2PIJ4; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000194221; 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; 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:UP000194221};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00379}.
FT DOMAIN 222..385
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 464
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 464 AA; 50902 MW; E1CA02C4CBE48550 CRC64;
MIQNDTIIAL ATPAGVGAIA VIRLSGEDAI KIVDSFFQSV KKQKSLLKQK SHTLHLGHIV
NNGITLDQVL VSIFKNPHSY TGENVVEISC HGSSFIQQEI IQLFLQNGCR MADNGEFTMR
AFLNGKMDLS QAEAVADVIA SNSAASHQMA IQQMRGGITN ELKELRAQLL DFAALIELEL
DFSGEDVEFA DRTKFKQLVA TISSVLKRLI DSFAFGNAMK NGIPVAIIGE PNVGKSTLLN
ALLNEEKAIV SDIAGTTRDA IEDEVIINGV AFRFIDTAGI RETEDIVESI GIKKAYEKAE
NAQLIIFLID SNKYIYSSDL FLEEITAVKE RFPNKRLLVI ANKIDTLSCH DTSIMQSEIE
NLILLSAKQK VGIDELKSEL TSLVNTGALS NNETIVTNSR HFEALTLALE SIESVKNGIE
LNISSDLFAI DIRECLRHLG NITGEYDVDK DILGHIFGNF CIGK
//
