ID A0A423X009_9PEZI Unreviewed; 555 AA.
AC A0A423X009;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=TrmE-type G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VPNG_05770 {ECO:0000313|EMBL:ROW09146.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW09146.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW09146.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW09146.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROW09146.1}.
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; LKEB01000032; ROW09146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423X009; -.
DR STRING; 1230097.A0A423X009; -.
DR InParanoid; A0A423X009; -.
DR Proteomes; UP000285146; Unassembled WGS sequence.
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 PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF103025; Folate-binding domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000285146};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 17..122
FT /note="GTP-binding protein TrmE N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10396"
FT DOMAIN 174..546
FT /note="MnmE helical"
FT /evidence="ECO:0000259|Pfam:PF12631"
FT DOMAIN 273..400
FT /note="G"
FT /evidence="ECO:0000259|Pfam:PF01926"
FT REGION 123..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 59394 MW; 3AECA889A4904BAC CRC64;
MSINNIGIIA GQAKNDTIYA LSSAQGRAGI AVIRMSGPAC LDIYQKLCPQ EPLPKPRYAH
LRTLYDPDSP DEKHILDSGA LVLFFPAPRT VTGENVLELH THGGPATVKA VLSAIPRCAS
AAGAARTGPG TGTGPGTGTG TGPGTGTGTG TGTIRYAEPG EFTKRAFLND RLDLSQVESL
GDVLDAETEQ QRRAAVRGTS GARGQAYDSW RGELLLARGE IEALIDFSED QHFDESPREL
LRNVTGMARR ILASIDVHEV AGQRTELLRK GVRIALLGPP NVGKSSLMNL VVGREASIVS
REAGTTRDVV EVSLDIGGYL CTFADTAGIR TRALESDGAI GSIEEEGIRR ARLKALSSDV
IVVLASVESR GDGGEPYINY DAETFELAAK AEQRIVVVNK CESVAKSELG HLLMAFKSQV
LDRVEGLAEE PLLISCKEAE TPSSSVEKDA GGIHHLTKHL IRSFENLTSL PEDLQELLGG
TERQRQLLAR CKEHLEDFMM EAVGDETESG RGTDDDEPDI VLAAEHLRYA GDCLAKITGR
GDAGDVEEVL GVLRW
//
