ID A9TQU1_PHYPA Unreviewed; 704 AA.
AC A9TQU1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN ORFNames=PHYPA_019425 {ECO:0000313|EMBL:PNR39147.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR39147.1};
RN [1] {ECO:0000313|EMBL:PNR39147.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c15_6620V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR39147.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c15_6620V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c15_6620V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; ABEU02000015; PNR39147.1; -; Genomic_DNA.
DR RefSeq; XP_001780981.1; XM_001780929.1.
DR AlphaFoldDB; A9TQU1; -.
DR STRING; 3218.A9TQU1; -.
DR PaxDb; 3218-PP1S291_62V6-1; -.
DR EnsemblPlants; Pp3c15_6620V3.1; Pp3c15_6620V3.1; Pp3c15_6620.
DR EnsemblPlants; Pp3c15_6622V3.1; Pp3c15_6622V3.1; Pp3c15_6622.
DR Gramene; Pp3c15_6620V3.1; Pp3c15_6620V3.1; Pp3c15_6620.
DR Gramene; Pp3c15_6622V3.1; Pp3c15_6622V3.1; Pp3c15_6622.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; A9TQU1; -.
DR OMA; WENPLAM; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000006727; Chromosome 15.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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:SF34; HEAT SHOCK PROTEIN 83; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727}.
FT DOMAIN 34..189
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 221..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 80742 MW; E1628FD5632B2FFC CRC64;
MADVTMSGPE VETFAFQAEI NQLLSLIINT FYSNKEIFLR ELISNSSDAL DKIRFESLTD
KSKLDGQPEL FIHIVPDKAN NTLSIIDSGI GMTKADMVNN LGTIARSGTK EFMEALSAGA
DVSMIGQFGV GFYSAYLVAE KVVVTSKHND DEQYIWESQA GGSFTITRDT SGEPLGRGTH
IKLYLKEDQL EYLEERRLKD LVKKHSEFIS YPISLWTEKT TEKEVSDDED EDDKKDEEGK
IEEVDEEKEK DKKKKKVKEI SREWTLINKQ KPIWMRKPED VTKEEYAAFY KSLTNDWEEH
LAVKHFSVEG QLEFKSVLFV PKRAPFDLFD SRKKQNNIKL YVRRVFIMDN CEELIPEYLG
FVKGVVDSED LPLNISRETL QQSKILKVIR KNLVKKCMEM FSEIAENKED YQKFYEAFSK
NLKLGIHEDS QNRSKLADLL RYHSTKSGDE MTSLKDYVTR MKEGQKDIYY ITGESKKAVE
NSPFLEKLKR RGYEVLFMVD AIDEYAVGQL KEFDGKKLVS ATKEGLVLED TEEEKKKKEE
KKARFEPLCK TIKDILGDKV EKVVVSDRIV DSPCVLVTGE YGWSANMERI MKAQALRDSS
MSSYMSSKKT MEINPDNQIM EELRKRAEVD KNDKSVKDLV LLLFETALLT SGFSLEEPNT
FGNRIHRMLK LGLSIDDDAT DADADMPALE ADVDEEGSKM EEVD
//
