ID A0A0R3PTI1_ANGCS Unreviewed; 707 AA.
AC A0A0R3PTI1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=HATPase_c domain-containing protein {ECO:0000313|WBParaSite:ACOC_0000908901-mRNA-1};
GN ORFNames=ACOC_LOCUS9090 {ECO:0000313|EMBL:VDM60675.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000908901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000908901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM60675.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM60675.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; UYYA01004246; VDM60675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3PTI1; -.
DR STRING; 334426.A0A0R3PTI1; -.
DR WBParaSite; ACOC_0000908901-mRNA-1; ACOC_0000908901-mRNA-1; ACOC_0000908901.
DR OMA; YMLQETS; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; 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; IPR019805; Heat_shock_protein_90_CS.
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:SF97; ENDOPLASMIN; 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.
DR PROSITE; PS00298; HSP90; 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:UP000267027}.
FT DOMAIN 28..187
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 669..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 81206 MW; 30E8A84157C614B8 CRC64;
MRAKAEQHEF QAEVNRMMKL IINSLYRNKE IFLRELISNA ADALDKIRLT SLTDPSALQT
NDDLSIRIKA DRENRLLHIT DSGIGMTKDE LMSNLGTIAR SGTAEFLSKL MDSSTSAEMQ
QDLIGQFGVG FYSAFLVADR VVVTTKSNDD EQYIWESDSG SFSIMKDPRG NTLKRGTQIT
LHMKEEANDF LEPDTLKNLV EKYSQFINFN IYLWQSKTET VDEPVEQEVV KTGEDGAVEE
EKEDKKTKKV EKTTWDWERV NNMKPIWMRK PSQVEPEEYD EFYKSITKDI EKPLAHVHFT
AEGEVSFKSI LYVPKRSPND MFQNYGKVIE NIKLYVRRVF ITDDFADMLP KYLAFIRGIV
DSDDLPLNVS RENLQQHKLL KVIKKKLVRK VLDMLKKLEG TQFDEFWSEF STNIKLGVME
DPSNRIRLAK LLRFASSADK EKLTSLTDYV QRMKEKQTKI YYMAGTSRKE VESSPFVERL
IAKGYEVLYL TEAVDEYCVQ AMPEFEGKKF QNVAKEGVSI DDSETAKEAF QALEKEFEPL
TTWLKETGLK GLIEKAVVSQ RLVKSPSALV ASIYGWSGNM ERIMKSQAYA KSKDPTQDFY
ANQKKTFEIN PRHPVVKELM RRVIADKEDQ KAKDTALLLF ETATLRSGYS LQDQVGFAER
IESVLRQSLD VDPDAEIEAE PVIEDTEDSK DTSTEEGTQV EEEHSEL
//
