FES1_KLULA
ID FES1_KLULA Reviewed; 289 AA.
AC Q6CNM7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Hsp70 nucleotide exchange factor FES1;
GN Name=FES1; OrderedLocusNames=KLLA0E11341g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
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.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Functions as a nucleotide exchange factor (NEF) for Hsp70
CC chaperones which accelerates the release of ADP. Required for fully
CC efficient Hsp70-mediated folding of proteins (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FES1 family. {ECO:0000305}.
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DR EMBL; CR382125; CAG99549.1; -; Genomic_DNA.
DR RefSeq; XP_454462.1; XM_454462.1.
DR AlphaFoldDB; Q6CNM7; -.
DR SMR; Q6CNM7; -.
DR STRING; 28985.XP_454462.1; -.
DR EnsemblFungi; CAG99549; CAG99549; KLLA0_E11375g.
DR GeneID; 2893735; -.
DR KEGG; kla:KLLA0_E11375g; -.
DR eggNOG; KOG2160; Eukaryota.
DR HOGENOM; CLU_046722_1_0_1; -.
DR InParanoid; Q6CNM7; -.
DR OMA; LHWSIAN; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013918; Nucleotide_exch_fac_Fes1.
DR Pfam; PF08609; Fes1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Repeat; Translation regulation.
FT CHAIN 1..289
FT /note="Hsp70 nucleotide exchange factor FES1"
FT /id="PRO_0000285396"
FT REPEAT 13..56
FT /note="ARM 1"
FT REPEAT 75..114
FT /note="ARM 2"
FT REPEAT 118..159
FT /note="ARM 3"
FT REPEAT 162..203
FT /note="ARM 4"
FT REPEAT 209..249
FT /note="ARM 5"
SQ SEQUENCE 289 AA; 32375 MW; 5262ABBD824EAC6B CRC64;
MEKLLHWSIA NAQGDDEAKA RAGQPDPKLL EQLFGGGPDE PTLMKHAMAV ISNPEATLEN
KLVAFDNFEM LIENLDNANN IENMKLWEPL ITVLDDPEPE LRAFALSVTG TAVQNNDQSQ
NNFAKYDGAL AKVIKLASGR AEDAQVRTKA FYTLSNLIRH NKLIYDQFNQ LNGLQIIAPV
LKDANASEKL KLRAMALLST VLTVADMNAD FFALLRAYNI IETTLEFLHP ECNLYLIDRV
LNFFSQLINV GFEFSATELE KLKVGVKNIE PVEAQLNEDD YKTVQYVSK