FES1_CANGA
ID FES1_CANGA Reviewed; 291 AA.
AC Q6FM01;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Hsp70 nucleotide exchange factor FES1;
GN Name=FES1; OrderedLocusNames=CAGL0K12144g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380957; CAG61706.1; -; Genomic_DNA.
DR RefSeq; XP_448743.1; XM_448743.1.
DR AlphaFoldDB; Q6FM01; -.
DR SMR; Q6FM01; -.
DR STRING; 5478.XP_448743.1; -.
DR EnsemblFungi; CAG61706; CAG61706; CAGL0K12144g.
DR GeneID; 2889971; -.
DR KEGG; cgr:CAGL0K12144g; -.
DR CGD; CAL0134753; FES1.
DR VEuPathDB; FungiDB:CAGL0K12144g; -.
DR eggNOG; KOG2160; Eukaryota.
DR HOGENOM; CLU_046722_1_0_1; -.
DR InParanoid; Q6FM01; -.
DR OMA; LHWSIAN; -.
DR Proteomes; UP000002428; Chromosome K.
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..291
FT /note="Hsp70 nucleotide exchange factor FES1"
FT /id="PRO_0000285389"
FT REPEAT 13..57
FT /note="ARM 1"
FT REPEAT 76..115
FT /note="ARM 2"
FT REPEAT 119..160
FT /note="ARM 3"
FT REPEAT 163..204
FT /note="ARM 4"
FT REPEAT 210..249
FT /note="ARM 5"
SQ SEQUENCE 291 AA; 32179 MW; 0B61590857314D0C CRC64;
MEKLLHWSIA NAQGDKEAIE KAGAPDPKLL EQLFGGGGPD DPTLMKEAMA VIMNPEADLE
NKLIAYDNFE MLIENLDNAN NIENMKLWEP ILKTLEDNEA DLRASGLSVI GTAVQNNTDS
QTNFLKYEGG LKILIAIAKS SEEPSDVRIK AFYALSNLLR NHIEAGKKFQ ALGGLDVFPV
ALNDPKATPK LKMRAISALS AFLSSSKIDE QLLDTLRKDG VLVSVIENLG TDNVNVIDRV
LSVLSHLISS GIKFNDSELE MLQKEFEKID SLKDRLNEDD YLAVKYVFSK K