ID J9A0D5_EDHAE Unreviewed; 541 AA.
AC J9A0D5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 08-NOV-2023, entry version 36.
DE RecName: Full=FACT complex subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=EDEG_00576 {ECO:0000313|EMBL:EJW05378.1};
OS Edhazardia aedis (strain USNM 41457) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Edhazardia.
OX NCBI_TaxID=1003232 {ECO:0000313|EMBL:EJW05378.1, ECO:0000313|Proteomes:UP000003163};
RN [1] {ECO:0000313|EMBL:EJW05378.1, ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|EMBL:EJW05378.1,
RC ECO:0000313|Proteomes:UP000003163};
RA Liu Z.J., Shi F.L., Lu J.Q., Li M., Wang Z.L.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USNM 41457 {ECO:0000313|Proteomes:UP000003163};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cuomo C.A., Sanscrainte N.D., Goldberg J.M., Heiman D., Young S., Zeng Q.,
RA Becnel J.J., Birren B.W.;
RT "Contrasting host-pathogen interactions and genome evolution in two
RT generalist and specialist microsporidian pathogens of mosquitoes.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJW05378.1}.
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DR EMBL; AFBI03000007; EJW05378.1; -; Genomic_DNA.
DR AlphaFoldDB; J9A0D5; -.
DR STRING; 1003232.J9A0D5; -.
DR VEuPathDB; MicrosporidiaDB:EDEG_00576; -.
DR HOGENOM; CLU_503450_0_0_1; -.
DR InParanoid; J9A0D5; -.
DR Proteomes; UP000003163; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF00183; HSP90; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000003163}.
FT REGION 151..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 61516 MW; C11D273855EA03C1 CRC64;
MIFVPAFEDN IMTTGKEPDP GSFEIFVHGC KLHKTLELPE FLKPFSFIIK SNDCNLSSSR
EDFLEPLMPT KLINELIKCV VELLIQQSDD DLFKMERIIK QGLIEAKKSN ADHKVIEKFM
GICAFETDKG NMSLFKFAEL LNSIEEEQRA LKKDNEEEKK DASDKENSKK TDNLKYPDYI
RYEEIYFTTV PSNLVKNTLN PTVDGAKAPF IFAATIMDEQ IIQAISTYRG KKFVDLSTKK
FINKKIVDDI NGKTKFKDLI DFITKKLANF ISSVEISEQL DKCPVKVQKG HGQISSAFKS
IIGVSKLESN PLRSFFEGKP VLQINTDHQD IIKINELIKL SKDSNDKKET SESKIEVETC
KETGNVVLKY NPLALAEESL ILMFFAATIT CGVDLYDKRN APLYLTNIVK KKLNLDVADI
VAEKSAFDFG SMANMFGGMG NNQDNTGNFD FGMDDHNDLE NLDNKDDQEN IEDSSEIADN
NHENVNDLEN EQEKNNKNEE VKTDQKEDAV ENQENKKINN EDQVKNDKEV PQIHDSVRDE
L
//
