ID A0A3G2QE10_9VIBR Unreviewed; 453 AA. AC A0A3G2QE10; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 17-JUN-2020, entry version 6. 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:AYO16115.1}; GN Synonyms=trmE {ECO:0000256|HAMAP-Rule:MF_00379}; GN ORFNames=APZ19_17285 {ECO:0000313|EMBL:QGH48740.1}, D0812_17620 GN {ECO:0000313|EMBL:AYO16115.1}; OS Vibrio owensii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=696485 {ECO:0000313|EMBL:AYO16115.1, ECO:0000313|Proteomes:UP000272136}; RN [1] {ECO:0000313|EMBL:QGH48740.1, ECO:0000313|Proteomes:UP000390336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH14 {ECO:0000313|EMBL:QGH48740.1, RC ECO:0000313|Proteomes:UP000390336}; RX PubMed=26634753; RA Liu L., Xiao J., Xia X., Pan Y., Yan S., Wang Y.; RT "Draft Genome Sequence of Vibrio owensii Strain SH-14, Which Causes Shrimp RT Acute Hepatopancreatic Necrosis Disease."; RL Genome Announc. 3:e01395-15(2015). RN [2] {ECO:0000313|EMBL:AYO16115.1, ECO:0000313|Proteomes:UP000272136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1700302 {ECO:0000313|EMBL:AYO16115.1, RC ECO:0000313|Proteomes:UP000272136}; RA Yan M., Wang X., Wang Y.; RT "Whole Genome of Vibrio owensii strain 170502, isolated from Acute RT Hepatopancreatic Necrosis Disease (AHPND) shrimp."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:QGH48740.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SH14 {ECO:0000313|EMBL:QGH48740.1}; RA Liang X., Wang Y.; RT "Complete genome sequence of Vibrio owensii SH-14 isolated from shrimp with RT acute hepatopancreatic necrosis diease."; RL Submitted (NOV-2019) 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|HAMAP- CC Rule:MF_00379, ECO:0000256|RuleBase:RU003313, CC ECO:0000256|SAAS:SAAS00534589}. 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; CP033137; AYO16115.1; -; Genomic_DNA. DR EMBL; CP045859; QGH48740.1; -; Genomic_DNA. DR RefSeq; WP_005440826.1; NZ_SMLI01000012.1. DR KEGG; vow:A9237_08320; -. DR KO; K03650; -. DR Proteomes; UP000272136; Chromosome 1. DR Proteomes; UP000390336; Chromosome 1. 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 Gene3D; 1.20.120.430; -; 1. DR Gene3D; 3.30.1360.120; -; 1. DR HAMAP; MF_00379; GTPase_MnmE; 1. DR InterPro; IPR031168; G_TrmE. DR InterPro; IPR018948; GTP-bd_TrmE_N. DR InterPro; IPR006073; GTP_binding_domain. 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 Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF12631; MnmE_helical; 1. DR Pfam; PF10396; TrmE_N; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 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|HAMAP-Rule:MF_00379, KW ECO:0000256|RuleBase:RU003313, ECO:0000256|SAAS:SAAS00027940}; KW 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|HAMAP-Rule:MF_00379, KW ECO:0000256|RuleBase:RU003313, ECO:0000256|SAAS:SAAS00272605}; KW Potassium {ECO:0000256|HAMAP-Rule:MF_00379}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00379, KW ECO:0000256|RuleBase:RU003313, ECO:0000256|SAAS:SAAS00272618}. FT DOMAIN 215..376 FT /note="TrmE-type G" FT /evidence="ECO:0000259|PROSITE:PS51709" FT NP_BIND 225..230 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT NP_BIND 244..250 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT NP_BIND 269..272 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT NP_BIND 334..337 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT METAL 225 FT /note="Potassium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT METAL 229 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT METAL 244 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT METAL 246 FT /note="Potassium; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT METAL 249 FT /note="Potassium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT METAL 250 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 22 FT /note="Formyltetrahydrofolate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 79 FT /note="Formyltetrahydrofolate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 119 FT /note="Formyltetrahydrofolate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 453 FT /note="Formyltetrahydrofolate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" SQ SEQUENCE 453 AA; 49214 MW; 9F66C5BD5169F460 CRC64; MTTDTIVAQA TAPGRGGVGI IRVSGPKANQ VALEVTGKTL KPRYAEYLPF QAEDGTVLDQ GIALYFPNPH SFTGEDVLEL QGHGGPVVMD MLIKRILGID GVRAARPGEF SERAFLNDKM DLTQAEAIAD LIDASSEEAA KSALQSLQGQ FSQRIQTLVE SLIHLRIYVE AAIDFPEEEI DFLADGKVSG DLQTIIDNLD AVRKEANQGA IMREGMKVVI AGRPNAGKSS LLNALSGKES AIVTDIAGTT RDVLREHIHI DGMPLHIIDT AGLRDASDEV EKIGIERAWD EIAQADRVLF MVDGTTTDAT DPKDIWPDFV DRLPNSIGMT VIRNKADQTG EDMGICHVND PTLIRLSAKT GAGVDALRTH LKECMGFSGN TEGGFMARRR HLDALERAAQ HLQIGQEQLE GYMAGEILAE ELRITQQHLN EITGEFSSDD LLGRIFSSFC IGK //