ID   HSP7F_ENCCU             Reviewed;         658 AA.
AC   Q8SQR8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Heat shock protein homolog SSE1;
GN   Name=SSE1; OrderedLocusNames=ECU11_1830;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Required for normal growth at various temperatures.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AL590450; CAD26093.2; -; Genomic_DNA.
DR   RefSeq; NP_586489.1; NM_001042322.1.
DR   AlphaFoldDB; Q8SQR8; -.
DR   SMR; Q8SQR8; -.
DR   STRING; 284813.Q8SQR8; -.
DR   GeneID; 860143; -.
DR   KEGG; ecu:ECU11_1830; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_1830; -.
DR   HOGENOM; CLU_415099_0_0_1; -.
DR   InParanoid; Q8SQR8; -.
DR   OrthoDB; 412565at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Calmodulin-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Stress response.
FT   CHAIN           1..658
FT                   /note="Heat shock protein homolog SSE1"
FT                   /id="PRO_0000383323"
FT   REGION          614..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..658
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  75189 MW;  871B3E5DE11F2C04 CRC64;
     MEFVGIDIGN YKTVIASSKE NGKVYGDEQG KRSIRTVMEL STPVRRFGNG VTNDVEQSLD
     LRSRSFRDAL EDKKGWGNLA MFMKYIDRVV KKNTPTHPPI CMAVPAYFKE RERRILVDIA
     NTMDFKLEGL ITDISAIAMF ACVRRENMPS EFLLFDFGFS KTTAGLFSFE KNVLKPLYMK
     TVRVGSMQFD EKLIDIIVEK HSLEKSRLVR EKIKRNLDKI KTTLNSTKCC NIQLFITENP
     LEVIITQEEY RNAVKSYLSD LDSFVSSVIK ETEFNGLVEV VGGNSISFLI KEMLRDKVEY
     QVTLDVSDST AIGAALGMAC MSLRTRYSLH DIVGREISIR IQGEDVSPTV IFKSTELVEG
     NPKIVTYNRK ESFVLEILED GEVISTLNVV KGETKETKAI HVSFSIGKFG TVCVNSVECE
     ESVDYEYKPF RISDIDLDDI KALEMKYRDG ELGLERIGTM RNELETMAVG LGDALYNKFG
     KITNDEELNT VREVAMDLFD MPQSETVGQE EEVRNTILSK LEFISKKLSD YRDAAVEDLK
     KHKDMINEFR KEYGSVFTPS FYKLQGLLYK VDEYLKDFDL NLFNVKLFDE SFIMEIKGDI
     QKYLEKAKLE IEEKRKEEER KSKKENAQEG TSSKPESKEE SEAKEDNDEE SDVASIDE