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Database: UniProt
Entry: D2VPU3_NAEGR
LinkDB: D2VPU3_NAEGR
Original site: D2VPU3_NAEGR 
ID   D2VPU3_NAEGR            Unreviewed;       708 AA.
AC   D2VPU3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=TNF receptor-associated protein {ECO:0000313|EMBL:EFC41267.1};
GN   ORFNames=NAEGRDRAFT_58871 {ECO:0000313|EMBL:EFC41267.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC41267.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC41267.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; GG738887; EFC41267.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2VPU3; -.
DR   STRING; 5762.D2VPU3; -.
DR   EnsemblProtists; EFC41267; EFC41267; NAEGRDRAFT_58871.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_58871; -.
DR   eggNOG; KOG0019; Eukaryota.
DR   InParanoid; D2VPU3; -.
DR   OMA; DHTQQNE; -.
DR   OrthoDB; 5485387at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
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; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL-RELATED; 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.
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   Receptor {ECO:0000313|EMBL:EFC41267.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          119..279
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
SQ   SEQUENCE   708 AA;  80282 MW;  A2953C4BF3D29634 CRC64;
     MLSRNSGKIV RSLVSKRSAA VRCSSSALPS SSSVLSKNSC SSYQQQQQLI ANFSSQLFVR
     NEKKDVIDDD VFEDAEVNEL KEENIIRETE HIVGAKENKT FETETKQLLH IVASALYTDK
     EVFIRELISN ASDALEKVRR MNQVSPDKVD DPSKELSVQI SCDDKNNIFV IQDSGIGMSK
     EELIKNIGTI AHSGSRAFVK QLKEASDKGE ATSNIIGQFG VGFYSTFMVA DKVRIYTRSA
     IKGQPGYCWE STGEGNYTIS EAEGVARGTK IVIYLKKNEK EFSFKDTVQK IIQKYSNFVS
     YPIILNGAKV NTLDAVWLKS KNSVTAEEHQ EFYKYLSHYG GNPLYILHFN LDIPLNMNAL
     FYVPDHHTES LGMGKMEPGV NVHSRRVLIR AKHPDILPDW LRFLKGVVDS EDLPLNISRE
     HLQDSPLIQK IKSVLVKRIT KFFNDMMKQD REKYISFYEK FNKFIKEGVV TDYMYKDEAA
     KLLMYESSAL PKGEKTTLEE YINRMGTEQK TIYYLIAPTR EYAENSPYFE VFKKKGIEVL
     FGYDGPDDFV FGSIGYFNGK ETKAIDRAEL EDDEADKTSG ENELSEIQSK ELCEWFQTSL
     KDKVSSAKIS KRLSTTPAVI KNPENASLRM IRKLQNQDIA LSPQQVEINP RHPLIMKLFN
     AKSANPDLAK LVAEQIFDNA LISAGLLDDP RSMVNRLQNL MESSLKSF
//
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