FES1_SCHPO
ID FES1_SCHPO Reviewed; 287 AA.
AC O43030;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Hsp70 nucleotide exchange factor fes1;
GN Name=fes1; ORFNames=SPBC3B9.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-20, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the FES1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17781.1; -; Genomic_DNA.
DR PIR; T40340; T40340.
DR RefSeq; NP_596658.1; NM_001022580.2.
DR AlphaFoldDB; O43030; -.
DR SMR; O43030; -.
DR BioGRID; 276819; 4.
DR IntAct; O43030; 2.
DR MINT; O43030; -.
DR STRING; 4896.SPBC3B9.01.1; -.
DR iPTMnet; O43030; -.
DR MaxQB; O43030; -.
DR PaxDb; O43030; -.
DR PRIDE; O43030; -.
DR EnsemblFungi; SPBC3B9.01.1; SPBC3B9.01.1:pep; SPBC3B9.01.
DR GeneID; 2540288; -.
DR KEGG; spo:SPBC3B9.01; -.
DR PomBase; SPBC3B9.01; fes1.
DR VEuPathDB; FungiDB:SPBC3B9.01; -.
DR eggNOG; KOG2160; Eukaryota.
DR HOGENOM; CLU_046722_1_0_1; -.
DR InParanoid; O43030; -.
DR OMA; LHWSIAN; -.
DR PhylomeDB; O43030; -.
DR PRO; PR:O43030; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISO:PomBase.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; ISO:PomBase.
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 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Translation regulation.
FT CHAIN 1..287
FT /note="Hsp70 nucleotide exchange factor fes1"
FT /id="PRO_0000285401"
FT REPEAT 75..114
FT /note="ARM 1"
FT REPEAT 117..157
FT /note="ARM 2"
FT REPEAT 160..200
FT /note="ARM 3"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 287 AA; 32745 MW; A6B9AD2E182BC0D1 CRC64;
MEKLLAFSTQ LQAQGNSSNS PPDPKDLDPS VLDHIFGANP ADEMRKAMDA IEDPSVPLDQ
KEIAFDNLEM LVEHIDNANN LVPLQLWPRL LKQLESPEST LRRLAAWTIA TAVQNNPKSQ
QALIENDGLK ILFGALKKED SDETKNKVLY AITSELKLNE AGIALLDKIP NSWEMLIEIL
ELKHSVMTKR VIFFFYALLI QEDKSKQIIL QKAHEFQIPE KVYQFSLEHS VDEDCVTKSL
HTLYLFQKNK VSVANTNELL KSLVQFKSEF PEIFTVDEWK AFHEALE
