ID A0A0D2F0Y5_9EURO Unreviewed; 955 AA.
AC A0A0D2F0Y5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE RecName: Full=Putative transferase CAF17, mitochondrial {ECO:0000256|ARBA:ARBA00018540};
DE AltName: Full=Putative transferase caf17, mitochondrial {ECO:0000256|ARBA:ARBA00016916};
GN ORFNames=PV05_09191 {ECO:0000313|EMBL:KIW53639.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW53639.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW53639.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW53639.1,
RC ECO:0000313|Proteomes:UP000054342};
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 xenobiotica CBS118157.";
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}.
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; KN847321; KIW53639.1; -; Genomic_DNA.
DR RefSeq; XP_013314223.1; XM_013458769.1.
DR AlphaFoldDB; A0A0D2F0Y5; -.
DR STRING; 348802.A0A0D2F0Y5; -.
DR GeneID; 25331099; -.
DR HOGENOM; CLU_308827_0_0_1; -.
DR OrthoDB; 5478664at2759; -.
DR Proteomes; UP000054342; 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.
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:UP000054342};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 400..531
FT /note="GTP-binding protein TrmE N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10396"
FT DOMAIN 534..952
FT /note="MnmE helical"
FT /evidence="ECO:0000259|Pfam:PF12631"
FT DOMAIN 634..764
FT /note="G"
FT /evidence="ECO:0000259|Pfam:PF01926"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 102948 MW; 6557747615B19A9E CRC64;
MSAEQETKST EETNIGGNLD AAGSASGAGS IGASANSKKS EEKRKPKKLG QKSSANGTPQ
KDEADTETNA GGDDEPPSTP APQPKMEQQS RSKSRQASRG RGRGSSQPPS DTDSAYRSDV
SQKGAKRNRN RNRGKAQAQS QAQSQDKDGG LLGGGGGPLD AVDEVGETVN GVADGAGDLV
NNTAGKALSK PHEALGGLLS NKKGGQEGEE EKDEGENEQL RLRLDLNLDI EVQLKAKIHG
DLTLGLLYCL IKRYALLVFT IVPQINAYPR RDHQSGQGPS CWWLVVVGMF VERLRCVTDV
DVSLHLGWLA KIGFSIISRR SYIFNAIIVV RMLCRFGTRS LVLSNYPAIC VSRPCFVRAA
SGAFPAPGLA SPRCRYASST VLPQVGNWHA QPEKQLTSET IYALSTAPGR AAIAVVRISG
SACLDIYRKI CPDRPLPKPR TATLRRLYDP EGIPTPRSQV LDNSALVLYF PAPNTVTGED
VLELHVHGGR AIVRSILDAI SACGRSLQES GNVIRHAEPG EFTKRAFYNG RLDLTQAEAL
GETLAAETEQ QRRLAVNGSD GGLAKRYEEW RLLLLYARGE LEALIDFSED QHFDESPAEF
LASVSTQVEA LKRQVEIHLQ NASKGELLRN GISIALLGAP NAGKSSLLNR IVGREAAIVS
AEEGTTRDIV DVSIDLQGWL CRLGDMAGLR ADVVGVGQSQ VGVVEQEGIR RARERALQSD
VVVALLSIEK TTEGTFDVPV NTKVFDAVQE CLTVGKTVLI VLNKVDLLKD ESRREEVLKN
LHMRVEEAFP MIPATRICAV SCKAAESSLN QTDVGGIQAF LGRLTNVFAE LTEAATSGDV
ENMAPAEAQS YWTSSLSVTH RQTTYLRQCL GHLDDFLDQS RPQIDSIAPA SDSYVDRHED
LAGPNDALQD EVDIVTAAEH LRFAADCLAT ITGKGQGGDV EDVLGVVFEK FCVGK
//
