EF1A3_MUCCL
ID EF1A3_MUCCL Reviewed; 457 AA.
AC P14865;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=TEF-3;
OS Mucor circinelloides f. lusitanicus (Mucor racemosus var. lusitanicus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=29924;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 1216b / BCRC 32522 / CBS 277.49 / NRRL 3631;
RX PubMed=3697088; DOI=10.1093/nar/15.23.9997;
RA Sundstrom P., Lira L.M., Choi D., Linz J.E., Sypherd P.S.;
RT "Sequence analysis of the EF-1 alpha gene family of Mucor racemosus.";
RL Nucleic Acids Res. 15:9997-10005(1987).
RN [2]
RP SEQUENCE REVISION.
RA Sundstrom P.;
RL Submitted (JAN-1990) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; X17475; CAA35506.1; -; Genomic_DNA.
DR AlphaFoldDB; P14865; -.
DR SMR; P14865; -.
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 Gene3D; 3.40.50.300; -; 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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW Protein biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT CHAIN 2..457
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090966"
FT DOMAIN 5..240
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 192..194
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 3
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 3
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 30
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 316
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 316
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT MOD_RES 389
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
SQ SEQUENCE 457 AA; 49836 MW; A6AF1F87D1577928 CRC64;
MGKEKTHVNV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAELG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETPKYNVTVI DAPGHRDFIK NMITGTSQAD CAILIIAGGT
GEFEAGISKD GQTREHALLA FTLGVRQLIV AINKMDTTKW SQDRYNEIVK EVSGFIKKIG
FNPKSVPFVP ISGWHGDNML DESTNMPWFK GWNKETKAGS KTGKTLLEAI DAIEPPVRPS
DKPLRLPLQD VYKIGGIGTV PVGRVETGTI KAGMVVNFAP AAVTTEVKSV EMHHETLTEG
LPGDNVGFNV KNVSVKDIRR GNVCSDSKND PAKESASFTA QVIILNHPGQ ISAGYAPVLD
CHTAHIACKF SELIEKIDRR SEKMEDSPKF VKSGDSAIVK MVPSKPMCVE AYTDYPPLGR
FAVRDMRQTV AVGVIKAVEK VDKAGKVTKA AAKASKK
