ID O61242_9ANNE Unreviewed; 374 AA.
AC O61242;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, 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 Laetmonice sp.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Errantia; Phyllodocida; Aphroditidae; Laetmonice.
OX NCBI_TaxID=73378 {ECO:0000313|EMBL:BAA25732.1};
RN [1] {ECO:0000313|EMBL:BAA25732.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9562984; DOI=10.1006/mpev.1997.0472;
RA Kojima S.;
RT "Paraphyletic status of Polychaeta suggested by phylogenetic analysis based
RT on the amino acid sequences of elongation factor-1 alpha.";
RL Mol. Phylogenet. Evol. 9:255-261(1998).
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|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; AB003703; BAA25732.1; -; mRNA.
DR PIR; T43829; T43829.
DR AlphaFoldDB; O61242; -.
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 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; 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; 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:BAA25732.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000325};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU000325,
KW ECO:0000313|EMBL:BAA25732.1}.
FT DOMAIN 1..196
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAA25732.1"
FT NON_TER 374
FT /evidence="ECO:0000313|EMBL:BAA25732.1"
SQ SEQUENCE 374 AA; 41409 MW; DDEA7F3BEBDF66FA CRC64;
QEMGKGSFKY AWVLDKLKAE RERGITIDIA LWKFETNKYY VTIIDAPGHR DFIKNMITGT
SQADCAVLIV AAGVGEFEAG ISKNGQTREH ALLAYTLGVK QLIIGINKMD STEPPYSETR
YQEIVKEVSA YIKKIGYNPD NVPFVPISGW HGDNMLEPSK YMQWFKGWKC KKGGKESNGN
TLLEALDVIE APKRPTDKPL RLPLQDVYKI GGIGTVPVGR VETGILKPGM LVTFAPCNLT
TEVKSVEMHH TALVEATPGD NVGFNVKNVS VKDVRRGNVA GDNKNDPPKE THEFRAQVII
LNHPGQISAG YAPVVDCHTA HIACKFKELM EKIDRRSGKK LEDNPQFVKS GDAAIVEMVP
QKPLCVEAFS QYPP
//
