ID A0A0V0WKP3_9BILA Unreviewed; 858 AA.
AC A0A0V0WKP3;
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=Heat shock protein 75 kDa, mitochondrial {ECO:0000313|EMBL:KRX76200.1};
GN Name=Trap1 {ECO:0000313|EMBL:KRX76200.1};
GN ORFNames=T06_2703 {ECO:0000313|EMBL:KRX76200.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX76200.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX76200.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX76200.1};
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
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:KRX76200.1}.
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DR EMBL; JYDK01000106; KRX76200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WKP3; -.
DR STRING; 92179.A0A0V0WKP3; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR007829; TM2.
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 Pfam; PF05154; TM2; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Signal {ECO:0000256|SAM:SignalP};
KW Stress response {ECO:0000313|EMBL:KRX76200.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..858
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006871919"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..416
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 858 AA; 97901 MW; 0BDE14E8035B603A CRC64;
MKYLDLIIFL LLVFMCITNA ANKFEKFNFC DFESFNEDAL PDSPLIPCNF LPEEFIVCDP
PLDLAGNETA KEILGYGCLK FGGVNSQDVE LTALKCQALP CIECQGPRTF LRQGFPCLRY
NGHYFLSALL YSIFLGFFAV DRFYLGYAGI GVGKLMTLGG LGVWWLVDIG LLISENEQLR
RKLKNGIFNQ SMHRMQVKRM LQTTTSVLAV VESECNSPIG IIIFDLTVLL LLLTSSEKHE
FRAETRMLLD VVANSLYSHK EVFVRELISN ASDALEKLRA LQATNATDIQ TVDELKIEIF
TNKLEKTFTI RDNGIGMTKE ELKSHLGTIA KSGTSDFVKK FKNSSHSNLE QFIGQFGVGF
YSAFMVADKI EVYTKARSPG SKGYRWVSDG NGYYEIEEVE NAEFGTKIVC HLKEGEAEFA
EESRIQDVIK KYSNFVSFPI MINEVKVNNM QALWLLDPKD VTKTMHKEFY RFISHSSNSE
PIFTFHFRVD APVNLNAILY VPDAVPDFLD MTHTEVGVLL YCRRVLIQQS AKDVIPNWLR
FLKGVIDSED IPLNLSRELL QKSSILNKIK SVTVSKVVKF FQDQMKKDAE NYEAFHSYYS
SYFREGILKS QSQIEKEDIA KLLLFESSNQ RPGKKVSFQD YCSRMQEDQR EIYYLCIPNR
SLAEASPYYE AVKADNLEIL FCYHPADEVT MISLRQFNRF NLVSVESVLQ RNRTENEVVE
TSDLSKEDLQ NMLEWIQKTL GQDKVNEIKT TQKITTYPCM ISILELGAVR SFLRANVMEK
MTDDQRLRLL KPTLEVNPNH PVIVKLAKLR FKDESLATAI LEQIYENALI AAGLVDNVQS
VVGKVNKLIS EVTQKLQT
//
