ID A0A0D2BJN2_9EURO Unreviewed; 625 AA.
AC A0A0D2BJN2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 37.
DE RecName: Full=Putative transferase CAF17, mitochondrial {ECO:0000256|ARBA:ARBA00018540};
DE AltName: Full=Putative transferase caf17, mitochondrial {ECO:0000256|ARBA:ARBA00016916};
GN ORFNames=PV06_10250 {ECO:0000313|EMBL:KIW37607.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW37607.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW37607.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW37607.1,
RC ECO:0000313|Proteomes:UP000053342};
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 Exophiala oligosperma CBS72588.";
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; KN847343; KIW37607.1; -; Genomic_DNA.
DR RefSeq; XP_016257823.1; XM_016411782.1.
DR AlphaFoldDB; A0A0D2BJN2; -.
DR STRING; 215243.A0A0D2BJN2; -.
DR GeneID; 27362324; -.
DR VEuPathDB; FungiDB:PV06_10250; -.
DR HOGENOM; CLU_019624_3_0_1; -.
DR OrthoDB; 5478664at2759; -.
DR Proteomes; UP000053342; 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:UP000053342};
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..622
FT /note="MnmE helical"
FT /evidence="ECO:0000259|Pfam:PF12631"
FT DOMAIN 302..433
FT /note="G"
FT /evidence="ECO:0000259|Pfam:PF01926"
FT REGION 556..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 67539 MW; 5B0BFCEF25A20B9A CRC64;
MICRGAWRAL SRSISTLRPC YDKVSFAKIV SAALPGSVGG SRSRYVSSTA ISDVRDWAPR
SADAFAPDTI YALSTAPGRA AIAVVRISGP ACLDIYRSLC PNRPQPKPRT ATLRRLYEPH
PNGAQSRQVL DNGALVLYFP ALNTVTGEDV LELHVHGGRA IVRSVLDAVS ACGGILKETG
YMIRPAEPGE FTKRAFYNGR LDLTQAEALG ETLAAETEQQ RRLAVSGSDG GLAKRYEEWR
TMLLYARGEL EALIDFSEDQ HFDESPVEFM ASVSEQVTGL QRQIEIHVRN ASKGELLRNG
INIALLGAPN AGKSSLLNRI VGREAAIVSA EEGTTRDIVD VSVDLQGWLC RLGDMAGLRS
GSGDNGQYRI GLVEREGIRR ARERALQSDV VVALLSIELD DEGTPIVPVN EQVYEAVQEC
HVAGKMILLV LNKIDLLENG AHRTAALQSL QAQVQKVFPT IPSNRICGIS CIDAESTMGT
QSSAGLQSFL HQLTDAFAEL TTAAAGGDID RINPAEAQAY WSASLSVTHR QSLYLKQCLG
HLNDFLDQAA PNSNVMSSSS VTKDSNRHEN TTIANHDPQD EIDIVTAAEH LRFAADCLAK
ITGTGETGDV EDVLGVVFEK FCVGK
//
