GenomeNet

Database: UniProt
Entry: R9XGF8_ASHAC
LinkDB: R9XGF8_ASHAC
Original site: R9XGF8_ASHAC 
ID   R9XGF8_ASHAC            Unreviewed;       842 AA.
AC   R9XGF8;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Elongation factor 2 {ECO:0000256|ARBA:ARBA00017891};
GN   ORFNames=AACERI_AaceriAFR142C {ECO:0000313|EMBL:AGO13289.1};
OS   Ashbya aceri (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=566037 {ECO:0000313|EMBL:AGO13289.1, ECO:0000313|Proteomes:UP000016920};
RN   [1] {ECO:0000313|Proteomes:UP000016920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; CP006025; AGO13289.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9XGF8; -.
DR   HOGENOM; CLU_002794_11_2_1; -.
DR   OrthoDB; 166721at2759; -.
DR   Proteomes; UP000016920; Chromosome VI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR   CDD; cd04096; eEF2_snRNP_like_C; 1.
DR   CDD; cd01885; EF2; 1.
DR   CDD; cd16261; EF2_snRNP_III; 1.
DR   CDD; cd03700; EF2_snRNP_like_II; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42908:SF10; ELONGATION FACTOR 2; 1.
DR   PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          17..253
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   842 AA;  93514 MW;  9A26C5230D87D867 CRC64;
     MVAFTVDQIR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK AGEARFTDTR
     KDEQERGITI KSTAISLFSE MTDDDVKDIK QKTEGNSFLI NLIDSPGHVD FSSEVTAALR
     VTDGALVVVD TVEGVCVQTE TVLRQALGER IKPVVVINKV DRALLELQVS KEDLYQSFSR
     TVESVNVIIS TYADEVLGDV QVYPQKGTVA FGSGLHGWAF TIRQFANRYS KKFGVDKEKM
     MDRLWGDSYF NPKTKKWTNK DRDADGKPLE RAFNMFVLDP IFRLFAAIMN FKKDEIPVLL
     EKLEISLKSD ERDLEGKALL KIVMRKFLPA ADALLEMIIL HLPSPVTAQN YRAEQLYEGP
     SDDPACIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV FSGTVKSGQK VRIQGPNFTP
     GKKEDLFIKA IQRAVLMMGR FVEPIDDCPA GNIVGLVGID QFLLKTGTLT TFESAHNMKV
     MKFSVSPVVQ VAVEVKNAND LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI
     CLQDLENDHA GIPLKISPPV VAYRETVEGE SSQVALSKSP NKHNRIYLKA QPIDEEVSLA
     IEGGKINPRD DFKARARVMA DEYGWDVTDA RKIWCFGPDG NGPNLVVDQT KAVQYLNEIK
     DSVVSAFQWA TKEGPIFGEQ MRSVRINLLD VTLHADAIHR GAGQIMPTMR RATYAGFLLA
     EPKIQEPVFL VEIQCPEQAV GGIYSVLNRK RGQVVSEEQR PGTPLFTVKA YLPVNESFGF
     TGELRQATGG QAFPQMVFDH WATLGTDPLD PTTKAGEIVV EARKRHGLKE TVPGWQEYYD
     KL
//
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