ID A0A0D2GLC9_9EURO Unreviewed; 644 AA.
AC A0A0D2GLC9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE RecName: Full=Putative transferase CAF17, mitochondrial {ECO:0000256|ARBA:ARBA00018540};
DE AltName: Full=Putative transferase caf17, mitochondrial {ECO:0000256|ARBA:ARBA00016916};
GN ORFNames=Z517_04774 {ECO:0000313|EMBL:KIW81748.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW81748.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW81748.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW81748.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-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}.
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DR EMBL; KN846971; KIW81748.1; -; Genomic_DNA.
DR RefSeq; XP_013285556.1; XM_013430102.1.
DR AlphaFoldDB; A0A0D2GLC9; -.
DR STRING; 1442368.A0A0D2GLC9; -.
DR GeneID; 25304264; -.
DR VEuPathDB; FungiDB:Z517_04774; -.
DR HOGENOM; CLU_019624_3_0_1; -.
DR OrthoDB; 5478664at2759; -.
DR Proteomes; UP000053029; 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 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:UP000053029};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 69..200
FT /note="GTP-binding protein TrmE N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10396"
FT DOMAIN 203..644
FT /note="MnmE helical"
FT /evidence="ECO:0000259|Pfam:PF12631"
FT DOMAIN 302..436
FT /note="G"
FT /evidence="ECO:0000259|Pfam:PF01926"
FT REGION 35..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 70245 MW; 6CDE6A50776B14CD CRC64;
MLYRIGFRSL SRHYLFSSAF RRCLAQPRGL NALRWSSSQP LPRGRSSSAP VPDLDEWSTR
ASQHTTSDTI YALSTASGRA AIAVIRISGP ACLQIYQQLC PNRGLPRPRT AALRKLYDPE
TARSSDPRVL DTGSLVLYFP APNTVTGEDV LEFHVHGGPA IVRSVLAAIA RCGHLMHGRE
GTVRHAEPGE FTKWAFYNGR LDLTQAEALG ESLAAETEQQ RRLAVSGADG GLAKRYEEWR
TMLLYARGEL EALIDFSEDQ HFDESPVEFV ASISKQVKAL KRQIELHLQN ASKGELLRNG
INVAFLGAPN AGKSSLLNQI VGREAAIVSA EEGTTRDIVD VSIDLNGWLC RLGDMAGLRA
TGTVGEQQQQ QLVGAVELEG IRRARERALQ SDVVLVLLPV EMDKDGNPQV PVNGEVLEAV
QQCDAAGKII LVVLNKIDLL GMHDDPRQEG MIALQTRIHQ IFPTVPERRI CLVSCKDATT
NVVGSDPGGI QAFLKQLTSS FMELTTPSAS EDIAEARLTA AEAQSYWTTS LSVTHRQTTY
LSQCLHHLED FLAQSQSRPQ SHLQMDTPEF SDSPDSATDY RTDRHNDLVA PNIAQVVGDG
DTDGAVDIVT AAEHLRFAAD CLAKITGKGG SGDVEDILGV VFEK
//
