ID A0A0V1BL91_TRISP Unreviewed; 816 AA.
AC A0A0V1BL91;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Endoplasmin {ECO:0000313|EMBL:KRY37564.1};
DE Flags: Fragment;
GN Name=HSP90B1 {ECO:0000313|EMBL:KRY37564.1};
GN ORFNames=T01_14445 {ECO:0000313|EMBL:KRY37564.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY37564.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY37564.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY37564.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
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:KRY37564.1}.
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DR EMBL; JYDH01000032; KRY37564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BL91; -.
DR Proteomes; UP000054776; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; 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; PF02518; HATPase_c; 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:UP000054776};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..816
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006875240"
FT DOMAIN 113..270
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 38..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY37564.1"
SQ SEQUENCE 816 AA; 94067 MW; AC8338E4BACB7BB0 CRC64;
LFIKVGMWNV PKQLWLILAV ALAVAIVECN FASANDKVKD DNDASPSVDP NLGKHKEGSR
TDDETIQREE EAIKLDGISV SQMKELRQKA EHHTFQAEVD RMMKLIINSL YKNKEIFLRE
LISNASDALD KIRLLSLTDP QAMETKPELS IRIKADKENN VLHITDTGIG MTKAELIGNL
GTIARSGTSQ FFKKFSEASP QEQQDLIGQF GVGFYSSFLV ADRVVVTSKH NNDTQHIWES
DAGSFNVFED PRGNELGRGT TVTLHIKEES QNFLEPNTLE ELVKKYSQFI NFNIYLWKSK
TVDVEESAEE EEKKEESPIE DEEGKVEEAA QEKPKKKKET KTVWDWELVN DTKPIWLRKA
ADIEEKEYQE FYKSLTKDYS SALAYTHFQA EGEVSFKSIL FIPERAPSDL YRESMKRNSN
IKLYVRRVFI SDEFEDFMPK YLAFIKGIVD SDDLPLNVSR ETLQQNKLIK VIRKKLVRKV
LDLLKKLPKE KFEKFWKEYS TVIKMGVFED PGNRQRLSKL LRFQSSNHPS DLTSLAEYVE
RMGERQKVIY YMAGTSRKEV ESSPFVERLL KKGIEVLYLV DPVDEYCMNS LPEFDNKKFQ
NVAKEGLSLE MSEKSKQRIA DLENDFSETL KWLKEDALKD KIEKAVLSQR LTKSPCALVA
SAWGWSGNME RLMRSQTYSK SQDPTQEYYM KEKKVFEINP YHPVIKAIKQ RVDEDKSDPL
ALSVARLLYD AATLRSGYLL KDSADFADRI DVMLKSALNL NPDEGAEEIE EDAEEDLPPI
PKEEPIDLDT YVPHFVKDDE KTKKEEESKK EEHNEL
//
