ID   A0A319C1T7_9EURO        Unreviewed;       675 AA.
AC   A0A319C1T7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Putative transferase CAF17, mitochondrial {ECO:0000256|ARBA:ARBA00018540};
DE   AltName: Full=Putative transferase caf17, mitochondrial {ECO:0000256|ARBA:ARBA00016916};
GN   ORFNames=BO82DRAFT_405871 {ECO:0000313|EMBL:PYH77730.1};
OS   Aspergillus uvarum CBS 121591.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH77730.1, ECO:0000313|Proteomes:UP000248340};
RN   [1] {ECO:0000313|EMBL:PYH77730.1, ECO:0000313|Proteomes:UP000248340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH77730.1,
RC   ECO:0000313|Proteomes:UP000248340};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ821737; PYH77730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319C1T7; -.
DR   STRING; 1448315.A0A319C1T7; -.
DR   VEuPathDB; FungiDB:BO82DRAFT_405871; -.
DR   OrthoDB; 5478664at2759; -.
DR   Proteomes; UP000248340; 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; IPR027266; TrmE/GcvT_dom1.
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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000313|EMBL:PYH77730.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          61..161
FT                   /note="GTP-binding protein TrmE N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10396"
FT   DOMAIN          235..343
FT                   /note="MnmE helical"
FT                   /evidence="ECO:0000259|Pfam:PF12631"
FT   DOMAIN          344..458
FT                   /note="G"
FT                   /evidence="ECO:0000259|Pfam:PF01926"
FT   REGION          165..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  72081 MW;  9211BB8B5D657CE7 CRC64;
     MRGFNLRTLR WAAAARPSLP VRNRAVSSRR SPAPLLLLNP SPRRCFSACR PNFSLFDADS
     TIYALSTAPG RAAIAVVRVS GPACVQIYNA LCPSAPLPRA RHAVVRTLYD PLQPPSSNTI
     LDAAALVLFF PGPRTVTGED VLELHLHGGP AIVKSVLTAI ANVNPSSSSL PSSSPSPTTT
     TTTHPKSPQV LLETPPRSGA AGGIEKGGGE GGGIIRYAEP GEFTRRAFLN NRLDLPQIEA
     LGEILHAETE QQRRIAVRAA SSSSGSGPDG AGALSQRYEQ WRHQLLYARG ELEALIDFAE
     DQHFDESPRQ LVGSVGRQVR ALQAQIRLHI GNAAKGELLR SGIRVALLGA PNAGKSSLLN
     RVVGREAAIV STEEGTTRDI VDVGVDVGGW FVRLGDMAGI RSEDVGEDDG EGRSSAARNV
     VIGAVEKEGI RRAKARALES DVVVVVVSLE AEQQQQQQQQ QQAGSAGSAS ASASRLAVER
     EVVDAANECA RAGRCVVVAI NKCDRLPGLD RLPDQLLATV RTLFPAVPAR RVFGISCLDA
     RRETGSVSGP AGHDPGHIQR FLQGLIATFE ELASPTGIEE DANGQYDRSY WEDSLGVTHR
     QSSNLQRCLE DLDAFMIQTQ SSNHDHHQLT PESDEEVDIV TAAEHLRSAA DALAKITGKD
     ESGDVEDVLG VVFEK
//