ID A0A1P6C609_BRUMA Unreviewed; 789 AA.
AC A0A1P6C609;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=BMA-ENPL-1, isoform b {ECO:0000313|EMBL:CDQ00792.2, ECO:0000313|WBParaSite:Bm5584a.1};
GN Name=bma-enpl-1 {ECO:0000313|WormBase:Bm5584b};
GN Synonyms=Bm1_39715 {ECO:0000313|WBParaSite:Bm5584a.1}, Bma-enpl-1
GN {ECO:0000313|EMBL:CDQ00792.2};
GN ORFNames=Bm5584 {ECO:0000313|WormBase:Bm5584b}, BM_Bm5584
GN {ECO:0000313|EMBL:CDQ00792.2};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CDQ00792.2};
RN [1] {ECO:0000313|EMBL:CDQ00792.2, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDQ00792.2,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CDQ00792.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDQ00792.2};
RG WormBase Consortium;
RA Ghedin E., Paulini M.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm5584a.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2022) to UniProtKB.
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; LN857014; CDQ00792.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P6C609; -.
DR EnsemblMetazoa; Bm5584a.1; Bm5584a.1; WBGene00225845.
DR WBParaSite; Bm5584a.1; Bm5584a.1; WBGene00225845.
DR WormBase; Bm5584b; BM26784; WBGene00225845; Bma-enpl-1.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000006672; 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; 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:UP000006672};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..789
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010812685"
FT DOMAIN 104..263
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 752..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..773
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 90894 MW; 3F331AC4F53C6818 CRC64;
MASNCAARLI VFIGVFFVLA FFPNTGVNAK VESNSEATVK ENIGRIKTSS KTDEEVIQRL
EEAIKLDGLS VAEMKELRIR AEKHSFQAEV NRMMKLIINS LYKNKEIFLR ELISNASDAL
DKIRLLSLTD PSVLSATDEL SVRIKADPEN HILHVTDTGI GMTKTDLINN LGTIARSGTS
EFLSKLLDSS TSLEQQQDMI GQFGVGFYSS YLVADRVVVT SKHNDDDQYV WESDSSSFIV
AKDPRGATLK RGTQVTLHLK EEAYDFLEAD TLKNLVEKYS QFINFNIYLW QSKTESVDEP
IEEVEKVNDE KTEDADGKVE EDKIEQKTKK VEKTTWDWEK INNVKPIWMR KNDDVEAEEY
TEFYKSITKD HENPLAYVHF TAEGEVTFKS ILYVPRHSPF DMFQNYGKGT DNIKLYVRRV
FITDDFHDIM PKYLSFIRGI VDSDDLPLNV SRETLQQHKL LKVIRKKLVR KVLDMFKKME
PSDFEDFWKE YSTNIKLGIM EDPTNRTRLA KLLRFYSSNG KGKMTSLAEY VSRMKDKQEM
IFYVAGNSRE EVESSPFVER LLKKGYEVLY LVEAVDEYTI QSMPEFDGKK FQNAAKEGLK
IDDGERSKGM QEQLEKEFEP LTDWLRNVAL KNKIEKALVS QRLVQSPCAL IASSYGWSGN
MERIMKSQAH SKSYDPTQEF YASQKKIFEI NPRHPVIKEL LRRVKSGESS EKATDTAVLL
FETATLRSGF TLNDQIGFAE RVEQILRRTI DVSLDEPVEE EPEIEEEDKD KEYVEEKDET
KDETEHSEL
//
