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Database: UniProt
Entry: F8MC28_NEUT8
LinkDB: F8MC28_NEUT8
Original site: F8MC28_NEUT8 
ID   F8MC28_NEUT8            Unreviewed;       246 AA.
AC   F8MC28;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Nucleotide exchange factor Fes1 domain-containing protein {ECO:0000259|Pfam:PF08609};
GN   ORFNames=NEUTE1DRAFT_75392 {ECO:0000313|EMBL:EGO60382.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO60382.1};
RN   [1] {ECO:0000313|EMBL:EGO60382.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO60382.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|ARBA:ARBA00024912}.
CC   -!- SIMILARITY: Belongs to the FES1 family.
CC       {ECO:0000256|ARBA:ARBA00011045}.
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DR   EMBL; GL891302; EGO60382.1; -; Genomic_DNA.
DR   RefSeq; XP_009847675.1; XM_009849373.1.
DR   AlphaFoldDB; F8MC28; -.
DR   GeneID; 20829802; -.
DR   KEGG; nte:NEUTE1DRAFT75392; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_75392; -.
DR   HOGENOM; CLU_084507_0_0_1; -.
DR   OrthoDB; 5473057at2759; -.
DR   Proteomes; UP000008065; Unassembled WGS sequence.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR013918; Nucleotide_exch_fac_Fes1.
DR   PANTHER; PTHR19316:SF18; HSP70-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR19316; PROTEIN FOLDING REGULATOR; 1.
DR   Pfam; PF08609; Fes1; 1.
DR   SMART; SM00185; ARM; 2.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
PE   3: Inferred from homology;
FT   DOMAIN          5..119
FT                   /note="Nucleotide exchange factor Fes1"
FT                   /evidence="ECO:0000259|Pfam:PF08609"
FT   REPEAT          165..193
FT                   /note="ARM"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT   REGION          22..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   246 AA;  26574 MW;  62989334AD40DAB3 CRC64;
     MDKNLNQLLK WSLEAQTAAN AGQSYNSNGA PTSNNNSGPA TGTGAVATSP APQVTGSGPR
     PVDPEVLASL FGGPSEAELM KAAMEVITDP SPETTRENKL IAFDNFEQLI ENLDNANLLE
     ELSLWSPLIS LLDHEDEDMR YHAAWCLGTA VQNNQKTQER LLAMGGVPKL VDLAMKEGES
     EKVRRKATYA LSSAVRNYQP AMDVAADEMH KRGHEVLVNN GTKVDAADMD KVDEVIDVLR
     NKAKSA
//
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