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Database: UniProt
Entry: A0A158QLT7_HAEPC
LinkDB: A0A158QLT7_HAEPC
Original site: A0A158QLT7_HAEPC 
ID   A0A158QLT7_HAEPC        Unreviewed;       674 AA.
AC   A0A158QLT7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=HATPase_c domain-containing protein {ECO:0000313|WBParaSite:HPLM_0000705901-mRNA-1};
GN   ORFNames=HPLM_LOCUS7051 {ECO:0000313|EMBL:VDO30791.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000705901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0000705901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO30791.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO30791.1,
RC   ECO:0000313|Proteomes:UP000268014};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UZAF01016592; VDO30791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158QLT7; -.
DR   STRING; 6290.A0A158QLT7; -.
DR   WBParaSite; HPLM_0000705901-mRNA-1; HPLM_0000705901-mRNA-1; HPLM_0000705901.
DR   OMA; DHTQQNE; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; Unassembled WGS sequence.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..674
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033730699"
FT   DOMAIN          71..222
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
SQ   SEQUENCE   674 AA;  76768 MW;  811AA736B1DCE541 CRC64;
     MWAARNALRP IAFLSTWPIR ARALRPLSVV VMQPHRSVTP SQRFYATAER HEFQAETKNL
     MDIVAKSLYS HSEVFVRELI SNASDALEKR RCVELTGEIA EGPSEIRVIT DEANRTITFE
     DTGIGMDRED LLECLGTIAK SGSKEFIEKN KDNAEAVIGQ FGVGFYSAFM VADSVVVTTR
     KVGAKEDQGL KWVWKGDNSY EISEESGLPT GTRVHIHLKA GDSADYSKAD KVKEYSYFVA
     APILLNGERV NSLNAIWTLQ PKDVTKEMHE TFFQQLAKQQ KKSDFIHRPC YTIHYKTDTP
     VSLRSVLYIP QHKFSMLEYA AQAHNRECGL SLYARRVLIK PNAGELLPNY LHFIMGVVDS
     EDVPLNLSRE MLQNNPVLRK LKKILTDKVL SFLQNEMKKD HEKYEEFYKY YNIFLKEGVV
     TEMEHSQKEE IAKLLLFESS NLKPGVLTNL SEYCKRMQEG QKEIFYMFSP SRQLAESSPY
     YELIKSQNKE VLFLYEPADE VVFLSMGQFQ MKSLIGIEKW AETAASTETG ETDTKQFRDI
     NKKELLDWIK TTLGSVKVHD IVGHHRPSDH PVMLTIKHEM GAARHLLRTG EIKDMEHLVF
     LQPCLHVNLS HPLIKSLYNM KRTDPQTAEL LISQVYDNAL ITSGLLKDTS GMVQRLNKLL
     TALAASGKST ILTP
//
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