EF1A_CRYNB
ID EF1A_CRYNB Reviewed; 459 AA.
AC P0CN31; O42671; O42672; Q55IA3; Q5K7T9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=TEF1; OrderedLocusNames=CNBM1160;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B-3501, and M1-106;
RX PubMed=9367655; DOI=10.1006/fgbi.1997.1002;
RA Thornewell S.J., Peery R.B., Skatrud P.L.;
RT "Cloning and molecular characterization of CnTEF1 which encodes translation
RT elongation factor 1alpha in Cryptococcus neoformans.";
RL Fungal Genet. Biol. 22:84-91(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000250}.
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:0000305}.
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DR EMBL; U81803; AAB88083.1; -; mRNA.
DR EMBL; U81804; AAB88586.1; -; Genomic_DNA.
DR EMBL; AAEY01000062; EAL17550.1; -; Genomic_DNA.
DR RefSeq; XP_772197.1; XM_767104.1.
DR AlphaFoldDB; P0CN31; -.
DR SMR; P0CN31; -.
DR PRIDE; P0CN31; -.
DR EnsemblFungi; AAW46945; AAW46945; CNM01300.
DR EnsemblFungi; EAL17550; EAL17550; CNBM1160.
DR GeneID; 4939476; -.
DR KEGG; cnb:CNBM1160; -.
DR VEuPathDB; FungiDB:CNBM1160; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR Proteomes; UP000001435; Chromosome 13.
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 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 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 2: Evidence at transcript level;
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..459
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000410069"
FT DOMAIN 5..240
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 192..194
FT /note="G5"
FT /evidence="ECO:0000250"
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 390
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02994"
FT VARIANT 84
FT /note="R -> K (in strain: M1-106)"
FT VARIANT 222
FT /note="K -> R (in strain: B-3501)"
FT VARIANT 231
FT /note="D -> S (in strain: B-3501)"
FT VARIANT 233..234
FT /note="IE -> SR (in strain: B-3501 and M1-106)"
FT VARIANT 236
FT /note="P -> H (in strain: B-3501)"
FT VARIANT 371
FT /note="A -> S (in strain: M1-106)"
FT VARIANT 404
FT /note="A -> S (in strain: M1-106)"
FT VARIANT 440..445
FT /note="DKTEKG -> EKSDGKS (in strain: M1-106)"
SQ SEQUENCE 459 AA; 50279 MW; 141AE9D27DBFDE2E CRC64;
MGKDKLHVNV VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQELG KSSFKYAWVL
DKLKAERERG ITIDIALWKF ETPRYQVTVI DAPGHRDFIK NMITGTSQAD CAILIIATGI
GEFEAGISKD GQTREHALLA FTLGVRQLIV ACNKMDTCKW SEDRFNEIVK ETNGFIKKVG
YNPKAVPFVP ISGWHGDNML EETTNMPWYK GWTKETKSGV SKGKTLLEAI DAIEPPTRPT
DKPLRLPLQD VYKIGGIGTV PVGRVETGVI KAGMVVKFAP TNVTTEVKSV EMHHEQIPEG
LPGDNVGFNV KNVSIKDIRR GNVCGDSKND PPMEAASFNA QVIVLNHPGQ IGAGYTPVLD
CHTAHIACKF AELIEKIDRR TGKVMEAAPK FVKSGDAAIV KLVAQKPLCV ETYADYPPLG
RFAVRDMRQT VAVGVIKSVD KTEKGGKVTK AAEKAAKKK
