ID Q9AVT7_PICAB Unreviewed; 444 AA.
AC Q9AVT7;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Elongation factor 1-alpha {ECO:0000256|RuleBase:RU000325};
DE Flags: Fragment;
OS Picea abies (Norway spruce) (Picea excelsa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3329 {ECO:0000313|EMBL:CAC27139.1};
RN [1] {ECO:0000313|EMBL:CAC27139.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Karst. {ECO:0000313|EMBL:CAC27139.1};
RX AGRICOLA=IND23279306;
RA Schubert R., Mueller-Starck G., Riegel R.;
RT "Development of EST-PCR markers and monitoring their intrapopulational
RT genetic variation in Picea abies (L.) Karst.";
RL Theor. Appl. Genet. 103:1223-1231(2001).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000256|ARBA:ARBA00003982, ECO:0000256|RuleBase:RU000325}.
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,
CC ECO:0000256|RuleBase:RU000325}.
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DR EMBL; AJ132534; CAC27139.1; -; mRNA.
DR AlphaFoldDB; Q9AVT7; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01883; EF1_alpha; 1.
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 HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00483; EF-1_alpha; 1.
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 PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Elongation factor {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:CAC27139.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:CAC27139.1}.
FT DOMAIN 2..227
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAC27139.1"
SQ SEQUENCE 444 AA; 49095 MW; F4D0B02DC7EA269D CRC64;
EKTHINIVVI GHVDSGKSTT TGHLIYKLGG IDKRVIERFE KEAAEMNKRS FKYAWVLDKH
KAERERGITI DIALWKFETN KYYCTVIDAP GHRDFIKNMI TGTSQADCAV LIIDSTTGGF
EAGISKDGQT REHALLAFTL GVKQMICCCN KMDATTPKYS KARYDEIVKE VSSYLKRVGY
NPDKIPFVPI SGFEGDNMIE RSTNLDWYKG PTLLEALDQV SEPKRPTDKP LRLPLQDVYK
IGGIGTVPVG RVETGIIKPG TIVTFGPTGL TTEVKSVEMH HEALQEAYPG DNVGFNVKNV
AVKDLKRGYV ASDSKNDPAK EAANFTAQVI IMNHPGQIGN GYAPVLDCHT CHIAVKFSEI
MTKVDRRSGK ELEKEPKFLK NGDAGFVKMI PTKPMVVETF AEYPPLGRFA VRDMRQTVAV
GVIKAVEKKD PTGAKVTKAA AKKK
//
