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Database: UniProt
Entry: A9QA78_9ASCO
LinkDB: A9QA78_9ASCO
Original site: A9QA78_9ASCO 
ID   A9QA78_9ASCO            Unreviewed;       309 AA.
AC   A9QA78;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Translation elongation factor 1-alpha {ECO:0000313|EMBL:ABX09924.1};
DE   Flags: Fragment;
OS   [Candida] nanaspora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX   NCBI_TaxID=51921 {ECO:0000313|EMBL:ABX09924.1};
RN   [1] {ECO:0000313|EMBL:ABX09924.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL Y-17679 {ECO:0000313|EMBL:ABX09924.1};
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; EU014711; ABX09924.1; -; Genomic_DNA.
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:ABX09924.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000313|EMBL:ABX09924.1}.
FT   DOMAIN          1..132
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABX09924.1"
FT   NON_TER         309
FT                   /evidence="ECO:0000313|EMBL:ABX09924.1"
SQ   SEQUENCE   309 AA;  33390 MW;  D607B9B4776845B2 CRC64;
     ADCAILIIAG GTGEFEAGXS KDGQTREHAL LAFTLGVRQL XVAVNKMDSV QWNEARFEEI
     IKETSXFIKK VGYNPKTVPF VPXSGWNGDN MIEPSANCPW YKGWQKETKA GVVKGKTLLE
     AIDAVEPPVR PSDKPLRLPL QDVYKIGGIG TVPVGRVETG VIKAGMVVTX APAGVTTEVK
     SVEMHHEQLV EGVPGDNVGF NVKNVSVKEI RRGNVCGXSK NDPPKGCXSF NAQVIVLNHP
     GQISAGYSPV LDCHTAHIAC KFDTLIEKID RRTGKSVEDS PKFVKSGDAA IVKMIPTKPM
     CVESFTEYP
//
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