ID Q6FTV4_CANGA Unreviewed; 207 AA.
AC Q6FTV4;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Candida glabrata strain CBS138 chromosome F complete sequence {ECO:0000313|EMBL:CAG59264.1};
GN Name=EFB1 {ECO:0000313|CGD:CAL0129370};
GN OrderedLocusNames=CAGL0F08547g {ECO:0000313|CGD:CAL0129370,
GN ECO:0000313|EMBL:CAG59264.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59264.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG59264.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC {ECO:0000256|ARBA:ARBA00007411, ECO:0000256|RuleBase:RU003791}.
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DR EMBL; CR380952; CAG59264.1; -; Genomic_DNA.
DR RefSeq; XP_446340.1; XM_446340.1.
DR AlphaFoldDB; Q6FTV4; -.
DR STRING; 284593.Q6FTV4; -.
DR EnsemblFungi; CAGL0F08547g-T; CAGL0F08547g-T-p1; CAGL0F08547g.
DR GeneID; 2887849; -.
DR KEGG; cgr:CAGL0F08547g; -.
DR CGD; CAL0129370; EFB1.
DR VEuPathDB; FungiDB:CAGL0F08547g; -.
DR eggNOG; KOG1668; Eukaryota.
DR HOGENOM; CLU_050172_0_2_1; -.
DR InParanoid; Q6FTV4; -.
DR OMA; YRWYKHI; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005829; C:cytosol; IDA:CGD.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:EnsemblFungi.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0005840; C:ribosome; IEA:EnsemblFungi.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:1990145; P:maintenance of translational fidelity; IEA:EnsemblFungi.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IEA:EnsemblFungi.
DR GO; GO:0006449; P:regulation of translational termination; IEA:EnsemblFungi.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR049720; EF1B_bsu/dsu.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR014717; Transl_elong_EF1B/ribsomal_bS6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR PANTHER; PTHR11595; EF-HAND AND COILED-COIL DOMAIN-CONTAINING FAMILY MEMBER; 1.
DR PANTHER; PTHR11595:SF21; ELONGATION FACTOR 1-BETA; 1.
DR Pfam; PF10587; EF-1_beta_acid; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM01182; EF-1_beta_acid; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF54984; eEF-1beta-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW ECO:0000256|RuleBase:RU003791};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU003791};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT DOMAIN 85..111
FT /note="Elongation factor 1 beta central acidic region
FT eukaryote"
FT /evidence="ECO:0000259|SMART:SM01182"
FT DOMAIN 121..207
FT /note="Translation elongation factor EF1B beta/delta
FT subunit guanine nucleotide exchange"
FT /evidence="ECO:0000259|SMART:SM00888"
FT REGION 68..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 22917 MW; 968F19B8C07E87AC CRC64;
MAFTDFSKID TVKELNTVLG EKSYVEGTSA TQADVEAYKA FRTAYPNFSR WFNHIAAKAD
EFDSFPAASG ASAAAEEEDD DDVDLFGSDD EVDEEAEKLK AQRLEEYNKR KAAKGPKPAA
KSIVTLDVKP WDDETDLEEM LANTKAVQMD GLNWGAHQFI PIGFGIKKLQ INCVVEDAKV
SLDDLQQAIE DDEDHVQSTD IAAMQKL
//
