ID A0A016WWU8_9BILA Unreviewed; 773 AA.
AC A0A016WWU8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN Name=Acey_s0471.g2056 {ECO:0000313|EMBL:EYC44140.1};
GN Synonyms=Acey-T05E11.3 {ECO:0000313|EMBL:EYC44140.1};
GN ORFNames=Y032_0471g2056 {ECO:0000313|EMBL:EYC44140.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC44140.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
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:EYC44140.1}.
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DR EMBL; JARK01000071; EYC44140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WWU8; -.
DR Proteomes; UP000024635; 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:UP000024635};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..773
FT /note="Histidine kinase/HSP90-like ATPase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001495120"
FT DOMAIN 92..251
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 288..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..757
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 88498 MW; 4A9D58382EB72D74 CRC64;
MRSRFVLLAL VALLATVAFY PTHVNAEDDI ETTESDKRKT DNDAAESEDD TIKIDGLTAA
QVKEMRAKAE KHEFQAEVNR MMKLIINSLY RNKEIFLREL ISNAADALDK IRLISLTDPS
ALHANEDLSV RIKADRENKL LHITDTGIGM TKDELMNNLG TIARSGTAEF LSKLMDSSTS
TDVQQDLIGQ FGVGFYSAFL VADRVVVTSK SNDGEQYIWE SDSGSFSITK DPRGPTLKRG
TQITLHMKEE AMDFLEPDTL KNLVHKYSQF INFNIYLWQS KTEMVEEPVE EEPKAKEDGA
VEEEKEEKKT KKVEKTTWDW ERVNNVKPIW MRKPSQVEPE EYEEFYKSIT KDTDKPLTHV
HFTAEGEVSF RSILYVPKKS PSDMFQNYGK IVENIKLYVR RVFITDDFAD MLPKYLAFIR
GIVDSDDLPL NVSRENLQQH KLLKVIKKKL VRKVLDMLKK LEGQEFDDFW KEFSTNIKLG
VMEDPSNRIR LAKLLRFASS ADKEKLTSLT DYVERMKDKQ DKIYYMAGIS RKEVETSPFV
ERLIAKGYEV LYLTEAVDEY CIQAMPEFDG KKFQNVAKEG VSIDDSEKAK EAYKELEKEF
EPLTSWLKET ALKDKIEKAV VSQRLVKSPS ALVASSYGWS GNMERIMKSQ AYAKAKDPTQ
EFYASQKKTF EINPRHPVVK ELLRRVAADK DDQKAKDTAT LLFETATLRS GFALQDQVGF
AERIESVLRQ SLDVAMDAEV EAEPTIDEQE EEQPAEEQPA AGETKVEEEH SEL
//
