HSP7B_ENCCU
ID HSP7B_ENCCU Reviewed; 683 AA.
AC Q8SSB1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Heat shock protein homolog ECU03_0520;
GN OrderedLocusNames=ECU03_0520;
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 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 -!- 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; AL590443; CAD26198.1; -; Genomic_DNA.
DR RefSeq; NP_597563.1; NM_001040927.1.
DR AlphaFoldDB; Q8SSB1; -.
DR SMR; Q8SSB1; -.
DR STRING; 284813.Q8SSB1; -.
DR GeneID; 858725; -.
DR KEGG; ecu:ECU03_0520; -.
DR VEuPathDB; MicrosporidiaDB:ECU03_0520; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; Q8SSB1; -.
DR OMA; GCKVQNA; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000000819; Chromosome III.
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 Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 2.
DR Pfam; PF00012; HSP70; 2.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..683
FT /note="Heat shock protein homolog ECU03_0520"
FT /id="PRO_0000383325"
SQ SEQUENCE 683 AA; 74830 MW; 9BB58CD959E4F39C CRC64;
MSEEKAKSNT SRAIGIDLGT TFSCVAGYIS GKVEVITNQD GERTTPSVVS FDENNCTVVG
TAARNMVGSD PMSVIFDAKR MIGREFDDPK IQNAIKGWPF KVVRYNHREK REEPNKVSEG
SNSYDNIAIK ITRNGKTNYY APVEISGKVL LYLKNAAEAR LGGTVDSAVV TVPAYFEEPQ
KDVTKAAATI AGFDPNKVRL LAEPTAAAMA YGHIQTQKNA NFSAKEDVLV FDLGGGTFDV
SLLDFEFNGA AGSLGIVKAI DGDTFLGGQD FDNLLINYCI SEFLKKNSSI KQSDLKESAL
LRLRAECTRV KAVLSSATSS AIYVPCFHMT DDLNVQITRA RFELLCDHLF RRCMERTKGC
LLRSAGVPEV EYSADGSKLL LNPSLEKTLN EVKNNISKVL LVGGSSRIPK IKALLAEYFG
AHKVIEPVNA DEAVAYGAAY QAASIYSDAV DAGSSLLLID CVPLNLSIET AGGVATALIH
CGDNIPIKKT ETFTTYEDNQ TAVTINVYEG NRAMCKDNKK IGSFNLDGII AAPRGVPKIE
VTFDVDHNGI LIVTAQDKQT GKENQIKVTN SQNRLSQEEI ERMTKEARDN EQRDNETKEK
MGKRMAFDQA ISSFKAFVEK ANNISEEKKS ESLRVIKENE EWLSNAQRPE DFEVEELERR
SNDFQSFTSD IMKDVGMGGA PAA