ID F0UR17_AJEC8 Unreviewed; 615 AA.
AC F0UR17;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Putative transferase CAF17, mitochondrial {ECO:0000256|ARBA:ARBA00018540};
DE AltName: Full=Putative transferase caf17, mitochondrial {ECO:0000256|ARBA:ARBA00016916};
GN ORFNames=HCEG_07559 {ECO:0000313|EMBL:EGC48344.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) 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}.
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DR EMBL; DS990641; EGC48344.1; -; Genomic_DNA.
DR AlphaFoldDB; F0UR17; -.
DR STRING; 544711.F0UR17; -.
DR VEuPathDB; FungiDB:I7I53_11031; -.
DR HOGENOM; CLU_019624_3_0_1; -.
DR OMA; IRGYLCT; -.
DR Proteomes; UP000008142; 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.
DR SUPFAM; SSF116878; TrmE connector domain; 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:UP000008142};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 63..195
FT /note="GTP-binding protein TrmE N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10396"
FT DOMAIN 198..604
FT /note="MnmE helical"
FT /evidence="ECO:0000259|Pfam:PF12631"
FT DOMAIN 297..430
FT /note="G"
FT /evidence="ECO:0000259|Pfam:PF01926"
SQ SEQUENCE 615 AA; 67672 MW; 13FC26F01338E528 CRC64;
MRRYFLQPLR WASIPGPPWT RSRCLSSING SQPCKPSLPR VRGQPGDKRW QTTASVVSEP
SSTIYALSTA PGRAAIAIVR VSGPACVQIY DALCPKRPLP NPRVAALRTL YDPSVPPSVN
TILDRAVVLH FPAPNTVTGE DVLELHIHGG PAVVKAVLNA IPRCAGAFSN EKIAMPSVRY
AEPGEFTRRA FLNDRLSLPQ IEALGNTLSA ETEHQRRLAV RGTSGSLAFR YERWRQQLLY
ARGEMEALID FSEDQHFDES IEEFVSSITG EVRNLVRQIN LHIENASKGE LLRSGIRVAL
LGAPNAGKSS LLNRIVGREA AIVSSEEGTT RDIVDVGVDI GGYFCKFGDM AGLRSGHIAR
SGSMPIGAVE QEGIRRAKAR ALESDVVIVV LSLEESDNGT GVKLVLEPEV VDAVRSCIAL
EKHMIVAVNK FDKYSPTTYT ARTQQKLVDS LTEEISSVEP RLTQDQIFLI SCREVENEVS
QEAEPGNIQK FLGELIRTFK RMSTPSELDN GNEQFDKLYW EDSLGVTHRQ RSNLQKCVQH
LNDFLSQTCQ TPDNAANAEQ IEVNFDIVTA AEHLRFAADC LAKITGRGES GDVEDVLGVV
FEKYSLPPIG PHFHS
//
