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Database: UniProt
Entry: A0A2Y9Q4E3_DELLE
LinkDB: A0A2Y9Q4E3_DELLE
Original site: A0A2Y9Q4E3_DELLE 
ID   A0A2Y9Q4E3_DELLE        Unreviewed;       806 AA.
AC   A0A2Y9Q4E3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Heat shock protein 75 kDa, mitochondrial {ECO:0000313|RefSeq:XP_022450442.1};
GN   Name=TRAP1 {ECO:0000313|RefSeq:XP_022450442.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022450442.1};
RN   [1] {ECO:0000313|RefSeq:XP_022450442.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022450442.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_022450442.1; XM_022594734.2.
DR   AlphaFoldDB; A0A2Y9Q4E3; -.
DR   STRING; 9749.A0A2Y9Q4E3; -.
DR   KEGG; dle:111185246; -.
DR   InParanoid; A0A2Y9Q4E3; -.
DR   OrthoDB; 5485387at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; 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; 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; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; 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   Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Stress response {ECO:0000313|RefSeq:XP_022450442.1}.
FT   DOMAIN          210..363
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  91773 MW;  38CDE98AC01B7A1C CRC64;
     MHKPRASWRR TSAPAAQRTR PSPLTTRHKV TEVPPPGPAA PTRPDRARTA PEPEPQRAPP
     TRRRRQRTGQ PGARCDVTTP RPKKAPPRPR PRHAWLLWAP RRTHMARELR TLLLWGCRLR
     DPALAVARGG KPVLCPWRPP AQSWSPRQNL ASSSHVGRRF SSQAAEDRKE EPLHSIISSS
     ETVQGSVSKH EFQAETKKLL DIVARSLYSE KEVFIRELIS NASDALEKLR HKLVSEGQTL
     PEMEIHLQTD AEKGTITIQD TGIGMTQEEL VSNLGTIARS GSKAFLDALQ SQAEASSKIV
     GQFGVGFYSA FMVADRVEVY SRSVDAGSPG YQWLSDGSGV FEIAEASGVR TGTKIIIHLR
     ADSREFTSEA RVRDVVTKYS KFVSFPLYMN GRRLNTLQAI WMMDPKDVGE GQHEEFYRYI
     AQAHDKPRYT LHYKTDAPLN IRSLFYVPET KPTMFDMSRE LGSSVSLYSR KVLIQTKATN
     ILPTWLRFIR GVVDSEDIPL NLSRELLQES ALIRKLQGVL QQRLIKFFID QSKKHAEKYA
     KFFEDYGLFM REGIVTTAEQ EVKEDIAKLL RYESSALPAG QLTSLPDYAS RMQAGTRSIY
     YLCAPNRHLA EHSPYYEAMK WKNTEVLFCY EQFDELTLLH LREFDKKKLM SVETDIVVDH
     YKEEKFEDGS PAGDRLSEKE TEDLMAWMRN ALGSRVTNVK VTLRLDIHPA MITVLEMGAA
     RHFLRMQQLA KTQEERAQLL QPTLEINPRH TLIKKLSQLR DSEPDLAQLL VDQIYENAMI
     TAGLVDDPRP MVSRLNHLLI KALDRH
//
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