ID A0A0L8GLG2_OCTBM Unreviewed; 794 AA.
AC A0A0L8GLG2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN ORFNames=OCBIM_22032112mg {ECO:0000313|EMBL:KOF77440.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF77440.1};
RN [1] {ECO:0000313|EMBL:KOF77440.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF77440.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF77440.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) 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; KQ421451; KOF77440.1; -; Genomic_DNA.
DR RefSeq; XP_014780250.1; XM_014924764.1.
DR AlphaFoldDB; A0A0L8GLG2; -.
DR STRING; 37653.A0A0L8GLG2; -.
DR EnsemblMetazoa; Ocbimv22032112m; Ocbimv22032112m.p; Ocbimv22032112m.g.
DR EnsemblMetazoa; XM_014924764.1; XP_014780250.1; LOC106876272.
DR GeneID; 106876272; -.
DR KEGG; obi:106876272; -.
DR OMA; YMLQETS; -.
DR OrthoDB; 547579at2759; -.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..794
FT /note="Histidine kinase/HSP90-like ATPase domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005583048"
FT DOMAIN 100..257
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 290..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..778
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 90878 MW; 86394808198C7B98 CRC64;
MLKQFTFLGI LWIVLWSACI SAAAASDETP EAVSVEESIG KSQDGSRTDD EVVKREEEAI
KLDGLNVAQM KELRDKAEKY AFQAEVNRMM KLIVNSLYKN KEIFLRELIS NASDALDKIR
FLAVTDQNAL AATEELSIKI KADKENHILH ITDTGIGMTK SDLVNNLGTI AKSGTSEFLK
KLDSSGSTEM SDLIGQFGVG FYSTFLVADK VMVTSKHNDD DQYIWESDSD SFQVLKDPRG
TTLARGTTIS LHLKEEAHDY LEENTLKDLI KKYSQFINFN IYLWTSKTEK VEEPVEDEEE
KPAEEKEEDE EEEGKVEEEK DEKPKTKTVE KTTWDWELLN SVKPIWTRKP NEITDDEYNA
FYKSISSDFT PPMAKIHFTA EGEVTFKSIL YVPKVSPSDT FNNYGKKADR IKMYVRRVFI
TDDFEDMMPK YLNFVSGVVD SDDLPLNVSR ETLQQHKLLK VIKKKLVRKT LDMIKKIDKE
EFASFWKEYS TNIKLGVIED PSNRTRLAKL LRFYSSNSET EQTSLAEYVE RMKEKQAAIY
FVAGASQKEV KNSPFVERLL KKGYEVLYLI EPVDEYCIQA LPEFEGKKFQ NVAKEGLSLS
DSENAKEKKE SLEKEYEPLL KWLKDDALSN QIEKATVSER LSSSPCALIA SQYGWSGNME
RIMRAQAYAK AKDSSQDYFA NQKRTLEINP RHKLIKMLKE KIESNKDDPT AKDLAVILFE
TATMRSGYLV PDTAGFAGRV ERMLRLSLNI EGEDMVEEEP EEQEEQVEQE EKVDADASET
DEKEEKVSHH SDEL
//
