ID B6U0V6_MAIZE Unreviewed; 807 AA.
AC B6U0V6;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Endoplasmin {ECO:0000313|EMBL:ACG42989.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACG42989.1};
RN [1] {ECO:0000313|EMBL:ACG42989.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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; EU970871; ACG42989.1; -; mRNA.
DR RefSeq; NP_001151475.1; NM_001158003.1.
DR AlphaFoldDB; B6U0V6; -.
DR OrthoDB; 547579at2759; -.
DR ExpressionAtlas; B6U0V6; baseline and differential.
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 2: Evidence at transcript level;
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..807
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002850560"
FT DOMAIN 100..257
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 292..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..793
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 92831 MW; 44F33C24E6B96A2C CRC64;
MRKWALSSAL LLLFLLTTLP DPAKKLQVNA EESSDDLANP PKVEEKLGAV PHGLSTDSEV
AQREAESISR KTLRSSAEKF EFQAEVSRLM DIIINSLYSN KDIFLRELIS NASDALDKIR
FLSLTDKEVL GEGDTAKLEI QIKLDKEKKI LSIRDRGIGM TKEDLIKNLG TIAKSGTSAF
VEKMQSGGDL NLIGQFGVGF YSVYLVADYV EVVSKHNDDK QYVWESKADG SFAISEDTWN
EPLGRGTEIR LHLRDEAKEY LEEDKLKDLV KKYSEFINFP IYLWSTKEVD VEVPTDEDET
SEEEDSTPET TEEETEEDED EEKEKKPKTK TIKETTSEWE LLNDVKAVWL RSPKEVTDEE
YSKFYHSLAK DFGDDKPMGW SHFTAEGDVE FKALLFIPPK APHDLYESYY NSNKSNLKLY
VRRVFISDEF DDLLPKYLSF LKGIVDSDTL PLNVSREMLQ QHSSLKTIKK KLIRKALDMI
RKLAEEDPDE YSNKDKTDEE KSEMEEKKGQ YAKFWNEFGK SIKLGIIEDA TNRNRLAKLL
RFESTKSDGK LASLDEYISR MKSGQKDIFY ITGSSKEQLE KSPFLERLTK KNYEVIFFTD
PVDEYLMQYL MDYEDKKFQN VSKEGLKLGK DSKLKDLKES FKELTDWWKK ALESENVDSV
KISNRLHDTP CVVVTSKYGW SANMEKIMQA QTLSDSSKQA YMRGKRVLEI NPRHPIIKEL
RDKVAQDNES EELKHTARLV YQTALMESGF NLPDPKEFAS SIYKSVQKGL DLSPDATVEE
DDEAEEQPEV EEKEPEPEPS SYDKDEL
//
