ID A9QAD1_9ASCO Unreviewed; 309 AA.
AC A9QAD1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Translation elongation factor 1-alpha {ECO:0000313|EMBL:ABX09977.1};
DE Flags: Fragment;
OS Peterozyma xylosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Peterozyma.
OX NCBI_TaxID=1337056 {ECO:0000313|EMBL:ABX09977.1};
RN [1] {ECO:0000313|EMBL:ABX09977.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL Y-12939 {ECO:0000313|EMBL:ABX09977.1};
RX PubMed=20522116; DOI=10.1111/j.1567-1364.2010.00625.x;
RA Kurtzman C.P., Robnett C.J.;
RT "Systematics of methanol assimilating yeasts and neighboring taxa from
RT multigene sequence analysis and the proposal of Peterozyma gen. nov., a new
RT member of the Saccharomycetales.";
RL FEMS Yeast Res. 10:353-361(2010).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR EMBL; EU014764; ABX09977.1; -; Genomic_DNA.
DR AlphaFoldDB; A9QAD1; -.
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:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:ABX09977.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:ABX09977.1}.
FT DOMAIN 1..132
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABX09977.1"
FT NON_TER 309
FT /evidence="ECO:0000313|EMBL:ABX09977.1"
SQ SEQUENCE 309 AA; 33387 MW; B5A03F3BC292B9F3 CRC64;
DCAILIIAAG IGEFEAGISK DGQTREHALL AYTLGVQQLI VAVNKMDSVK WSESRFDEIS
KETASFIKKV GYNPKTVPFV PISGWNGDNM IDSSPNCPWY KGWVKETKAS GVVKGKTLLD
AIDAIEPPVR PTEKPLRLPL QDVYKIGGIG TVPVGRVETG IIKAGMIVTF APAGVTTEVK
SVEMHHEQLA QGVPGDNVGF NIKNVSVKEI RRGNVCGDSK NDPPKAAESF TAQVIVLNHP
GQISAGYSPV LDCHTAHIAC KFDTLIEKID RRTGKVMEAN PKYIKSGDAA IVKMVPSKPM
CVEAFTQYP
//
