ID A0A176W231_MARPO Unreviewed; 724 AA.
AC A0A176W231;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Histidine kinase/HSP90-like ATPase domain-containing protein {ECO:0000259|SMART:SM00387};
GN ORFNames=AXG93_900s1100 {ECO:0000313|EMBL:OAE27124.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE27124.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE27124.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE27124.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OAE27124.1}.
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DR EMBL; LVLJ01001973; OAE27124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176W231; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF02518; HATPase_c; 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:UP000077202}.
FT DOMAIN 32..187
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 224..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 83176 MW; 7F5DCFDB2A732BCF CRC64;
MGAEDVLDVE TFAFQAEINQ LLSLIINTFY SNKEIFLREL ISNSSDALDK IRFEGLTDKS
KLESQPELFV HIIPDQVNNS LTIIDSGIGM TKTDLVNNLG TIARSGTKSF MEALSAGADI
SMIGQFGVGF YSAYLVAERV VVHTRHNDDD QYIWESQAGG SFTVRKDTSG EPLGRGTKVV
LMLKEDQLEY LEEKRLKDLV KKHSEFISYP ISLWTEKTVD KEVSDDEEEV VDRKGKGIKE
EDDAASDGDV DTEGRIEEVP EDETEKKETV TRKKKKVKEV THEWAQINKM KPIWMRNPEE
ISREEYAAFY KSLTNDWEEH LSVKHFSVEG QLEFKSVLFI PKRAPFDMFD QRKKQNNIKL
YVRRVFIMDN CEEVIPEYLG FVKGIVDSED LPLNISREML QQNKILKVIR KNIVKKCLEM
FNEIAESKDD YKTFYETFGK NLKLGIHEDS QNRAKLADLL RYQSTKCGDE YTSFKDYVTR
MKDGQKDIYL ITGESRKAVE NSPFLEQLKK RGYEVLFMVD PIDEYAVQQL KDYDGHKLVS
ATKEGLKLED TEENLKKKEE IKARFESLCK VMKEILGEKV EKVLVSDRIV DSPCCLVTGE
YGWTANMERI MKAQALRDNS MSNYMSSKKT LEVNPENQIM IEIQKRAEAD KTDKTVKDLV
LLLFETALLT SGFSLDEPNT FGTRIHRMIK LGLSIDEDAV PVEDDVEMPP LEEDDEGSRM
EEVD
//
