ID   A0A1L8EYC8_XENLA        Unreviewed;       709 AA.
AC   A0A1L8EYC8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Heat shock protein 75 kDa, mitochondrial {ECO:0000313|RefSeq:XP_018092019.1};
GN   Name=trap1.L {ECO:0000313|RefSeq:XP_018092019.1,
GN   ECO:0000313|Xenbase:XB-GENE-999252};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018092019.1};
RN   [1] {ECO:0000313|RefSeq:XP_018092019.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018092019.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018092019.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_018092019.1; XM_018236530.2.
DR   AlphaFoldDB; A0A1L8EYC8; -.
DR   STRING; 8355.A0A1L8EYC8; -.
DR   PaxDb; 8355-A0A1L8EYC8; -.
DR   GeneID; 100380995; -.
DR   KEGG; xla:100380995; -.
DR   AGR; Xenbase:XB-GENE-999252; -.
DR   CTD; 100380995; -.
DR   Xenbase; XB-GENE-999252; trap1.L.
DR   OMA; DHTQQNE; -.
DR   OrthoDB; 5485387at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 100380995; Expressed in neurula embryo and 19 other cell types or tissues.
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; 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   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
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:UP000186698};
KW   Stress response {ECO:0000313|RefSeq:XP_018092019.1}.
SQ   SEQUENCE   709 AA;  80541 MW;  056BA3B0407D8A3A CRC64;
     MATGALLRGV VSRALRGRCL PLSRKQGRSV SVCSSRGPTA AWHPLTVSRT GPPTLCAADR
     RSYTTQASET KEEELLHTII CDTENVQGAA SKHEFQAETK KLLDIVARSL YSEKEVFIRE
     LISNGSDALE KLRHKHLAQG SSLAEMEIHL QTDGDKGTLT IQDTGVGMNM DELISNLGTI
     ARSGSKAFLD ALQNQADSSS KIIGQFGVGF YSAFMVADKV VVYSQSSEAG SPGYCWSSDG
     SGVFEIVEAN GVRPGTKVVI HLKDDCKEFA NEDRVKEVIT KYSNFVSFPL YLNGKRINTL
     QALWMMDPKE IGEWQHEEFY RFIAQAYDKP RYMLHYKADA PLNIRSIFYV PEMKPSMFDV
     SREMGSSVSL YSRKVLIQTK AADILPKWLR FLRGIVDSED IPLNLSRELL QESVLIRKLR
     DVLQKRLIKF FIDRSKKDPE KYGKFFEDYG LFMREGIVTT AEQEVKEDIA KLLRFESSSL
     PEGQQTSLTE YASRMQPGTR NIYYLCAPNR HLAEHSPYYE AMKKKQTEVL FCYEQFDELT
     MLHLREFDKK KLISVETDIV VDHYKEEKFE ESIPASERLS EKEAEDLMAW MRNGLGTRIT
     NVKVTPRLDT HPAMITVLEM GAARHFLRTQ QLAKTSEERA QILQPTLEIN TGHPLIKKLW
     QLKDGEQELA KLLLDQIYEN AMIAAGLNED PRPMIGRLNE LLTKAFDKH
//