GenomeNet

Database: UniProt
Entry: A0A1I5RDS9_9SPHN
LinkDB: A0A1I5RDS9_9SPHN
Original site: A0A1I5RDS9_9SPHN 
ID   A0A1I5RDS9_9SPHN        Unreviewed;       438 AA.
AC   A0A1I5RDS9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN04488241_103187 {ECO:0000313|EMBL:SFP56615.1};
OS   Sphingomonas rubra.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=634430 {ECO:0000313|EMBL:SFP56615.1, ECO:0000313|Proteomes:UP000199586};
RN   [1] {ECO:0000313|EMBL:SFP56615.1, ECO:0000313|Proteomes:UP000199586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9113 {ECO:0000313|EMBL:SFP56615.1,
RC   ECO:0000313|Proteomes:UP000199586};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00379}.
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; FOXP01000003; SFP56615.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5RDS9; -.
DR   STRING; 634430.SAMN04488241_103187; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000199586; 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; 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.
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:UP000199586};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00379}.
FT   DOMAIN          17..131
FT                   /note="GTP-binding protein TrmE N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10396"
FT   DOMAIN          134..435
FT                   /note="MnmE helical"
FT                   /evidence="ECO:0000259|Pfam:PF12631"
FT   DOMAIN          231..318
FT                   /note="G"
FT                   /evidence="ECO:0000259|Pfam:PF01926"
FT   BINDING         34
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         91
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         131
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         239..244
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         239
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         258..264
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         258
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         260
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         263
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         283..286
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         438
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   438 AA;  45801 MW;  0BF7BF69E2772D9F CRC64;
     MATAAGRHDE ARGVTDTIVA LSSGRPPAAI GVIRVSGPAA LVAAATLAGT LPPPRIAGLR
     ALRDANGAML DRALVLVFPG SRSATGEDLV EFHCHGGRAV IAAVEAALVA ATGCRAALPG
     EFTRRALTNG RIDLAEAEGL ADLLEAETEA QRVAALAAAE GRISRQVATW MASAAAISAR
     IEALIDHDDE GDVETGEEVL AAIMADAAVL GTEIAFAVEA PPVERLRDGV RVVIAGPPNA
     GKSTLLNLLG EREAAIVSPI AGTTRDMVEA PVVRRGRAFV LTDTAGLTRS DDVVEMIGVD
     RARYAIEAAD ILLWLGDEPP PRDDAIPIHS RADAAERRVV PAGRLAISRD APRSIESLWN
     VIEERASALL PRIDGLPWRQ RHQQLCGEAA AALLQGSNDP VLLAENCRTA RVRLAAIVGI
     DATEAMLDAL FSRFCLGK
//
DBGET integrated database retrieval system