ID C5KHG1_PERM5 Unreviewed; 811 AA.
AC C5KHG1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Endoplasmin, putative {ECO:0000313|EMBL:EER16023.1};
GN ORFNames=Pmar_PMAR003486 {ECO:0000313|EMBL:EER16023.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER16023.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; GG673069; EER16023.1; -; Genomic_DNA.
DR RefSeq; XP_002784227.1; XM_002784181.1.
DR AlphaFoldDB; C5KHG1; -.
DR EnsemblProtists; EER16023; EER16023; Pmar_PMAR003486.
DR GeneID; 9061009; -.
DR InParanoid; C5KHG1; -.
DR OMA; KWKLMNE; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
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; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..811
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005668552"
FT DOMAIN 62..219
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 177..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..283
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..811
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 92423 MW; 418F6D467EDDDFD0 CRC64;
MRFQRLFAVL LLPLVAVFAE EKASVGSTQD LAAEYEDHAE KHEFQAEVSR LMDIIINSLY
THKEVFLREL ISNANDALEK ARYNSLQDPD YLKEKPELDI KIDYDENANT LTITDSGVGM
TKADLINNLG TVAKSGTSNF LEAMAEGGSD ANLIGQFGVG FYSAFLVADK VSVASKNNDD
PEQHIWESSA DASFSVGPDP RGDTLGRGTE ITLHLKEDAH EYLEESRLKD LATKYSQFVP
YSISLKTKKE VEADLDEDEE ESDESQKEDS DVEVKEEDES EEEDKEKEKT RKKQTVYDYE
QVNTQKALWL RNKEDITDED YEQFYMAIAK DHAGPLAYTH FSAEGEIEFK AILFVPKRTP
YNFMQNYWEK KSEIKLYVRR VLVADKFDEL LPRYLNFITG VVDSDDLPLN VSREQLQQNK
ILKVISKKLV RKVLEMIKKL AMAKVDEAAE TEEKDKSSKD KETDWGEASS KRACQSGVIH
LDKFYSSFAD NLKLGCFEDD ANRSKIAKLL RFRTTKSGDK SISLDKYIEN MDENQDSIYY
MSGDSIDVMV KNPSLQIFNK KGIEVLLLDN HLDEPCMQRL TDYDGKKLVS IQKADVKLEE
TEDDKKRFSK LQKMYKPLTK WYKDILTKAS EKDPQANYNY GVESVKISKR LVDAPCVVVS
DQFGYTPQQE RVVRAQSFQD KTQLNMMIGR RTLELNPDHP VIKDLLVKVN EDKADTNAED
TAVVLFQAAM LDSGYEILDP HTLVKKVYSL MSQSLGVDPN TPVAEVEVPE DEEEVEEPPA
EEESDDSTTI GEEEELEPDN EMSKESEDEE L
//
