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Database: UniProt
Entry: A0A372IGC1_9RHOB
LinkDB: A0A372IGC1_9RHOB
Original site: A0A372IGC1_9RHOB 
ID   A0A372IGC1_9RHOB        Unreviewed;       427 AA.
AC   A0A372IGC1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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   ECO:0000313|EMBL:RFU13801.1};
GN   Synonyms=trmE {ECO:0000256|HAMAP-Rule:MF_00379};
GN   ORFNames=DZD18_05540 {ECO:0000313|EMBL:RFU13801.1};
OS   Rhodobacteraceae bacterium W635.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2303578 {ECO:0000313|EMBL:RFU13801.1, ECO:0000313|Proteomes:UP000264655};
RN   [1] {ECO:0000313|EMBL:RFU13801.1, ECO:0000313|Proteomes:UP000264655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W635 {ECO:0000313|EMBL:RFU13801.1,
RC   ECO:0000313|Proteomes:UP000264655};
RA   Hou X.J.;
RT   "Ayaqqumibacter halotolerans gen. nov., sp. nov., isolated from a saline
RT   lake in Xinjiang province, China.";
RL   Submitted (AUG-2018) 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:RFU13801.1}.
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DR   EMBL; QVQC01000029; RFU13801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372IGC1; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000264655; 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|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:UP000264655};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00379}.
FT   DOMAIN          213..350
FT                   /note="TrmE-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51709"
FT   BINDING         20
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         77
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         117
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         223..228
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         223
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         242..248
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         242
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         244
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         247
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         267..270
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         427
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   427 AA;  45535 MW;  B7852CBDB6E30DB3 CRC64;
     MDTIFALATA PGKAGVAVIR ISGPEAFAVG RGLAGKLPNV GEARMRRLSN AEGAHLDDAL
     VLAFKAPHSF TGEDVVELQT HGSPATIKAV LAAISETGMA RMAEPGEFTR RALENDRMDL
     AQVEGLADLI DAETELQRLQ ALRVLSGGLG QLVEQWRENL LRAAALLEVT IDFADEEVPV
     DVAPDVISLL EPIMDDLRRE IAGVNVAERI RDGFEVAILG APNVGKSTLL NALAGREAAI
     TSDIAGTTRD VIEVRMDLNG LPVTVLDTAG LRESEDAVER IGVDRARSRA DAADLRVFLK
     SLPGEKPNIT LSDEDIVLLG KADLHGQEGV SGVTGQGVSG LVHRITETLS TRAARQSTAT
     HARHAEAMRD AVKALESGLN EVQAGADRTE LAAEHLRMAI RRLDSLIGRI DVEMVLGEIF
     SRFCLGK
//
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