ID   A0A2G5I363_CERBT        Unreviewed;       598 AA.
AC   A0A2G5I363;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   SubName: Full=tRNA modification GTPase MnmE {ECO:0000313|EMBL:PIA99239.1};
GN   ORFNames=CB0940_03141 {ECO:0000313|EMBL:PIA99239.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA99239.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA99239.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA99239.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. TrmE GTPase family.
CC       {ECO:0000256|ARBA:ARBA00011043}.
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:PIA99239.1}.
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DR   EMBL; LKMD01000101; PIA99239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5I363; -.
DR   OrthoDB; 5478664at2759; -.
DR   Proteomes; UP000230605; Chromosome 3.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          69..196
FT                   /note="GTP-binding protein TrmE N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10396"
FT   DOMAIN          199..595
FT                   /note="MnmE helical"
FT                   /evidence="ECO:0000259|Pfam:PF12631"
FT   DOMAIN          298..434
FT                   /note="G"
FT                   /evidence="ECO:0000259|Pfam:PF01926"
SQ   SEQUENCE   598 AA;  64847 MW;  9DD1F853007A3D25 CRC64;
     MRKILSSFAR IARPCSRTPS GLVSPRRWIF EHARSVTPTR TRQCLLHASQ HVGSKGSASA
     ASNTYTEPTI YALSTAPGRA AIAVIRVSGP ASLQIYHALC PGKKPPKSRV ATVRTLYDPS
     GPPSQDSVLD SSALVLYFEG PTTATGEDVL ELHVHGGPAI VKAILAAISR CRTSSGSMIR
     YAEPGEFTRR AFMNKRLDLT QVESLGDTLA ADTEQQRRLS VRGTTGSLAK QYEAWRQQLL
     YARGELEALI DFSEDQHFDE SPSELMTSVA AQVEVLRKSL LIHSQNAVRG ELLRHGIKIS
     LLGAPNAGKS SLLNRIVGRE AAIVSNEAGT TRDIVEIGLD LGGYLCRFGD TAGLRRAIEA
     DLGSGKSAEK INQIEQEGMR RAKARAEESD LVVVVFSFEQ TEDGRICLNL DPEVCQMAER
     LKSEGKNVVV VVNKADLVHD GTSVDVDAIQ HIRKRLPLVA DESIQVLSCL DTDEARNALR
     SFLKGLVTEF EKLTAAISPE LGIDGHSPDQ SIWQESLGAS ERHRLLLDQC IAALDQFMSE
     AQVESKSTMN EGEEADIVLA AEHLRAAADC LAKITGKGES GDVEEVLGVV FEKFCVGK
//