ID A0A176VZB0_MARPO Unreviewed; 350 AA.
AC A0A176VZB0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein {ECO:0000259|SMART:SM01000};
GN ORFNames=AXG93_4022s1090 {ECO:0000313|EMBL:OAE26097.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE26097.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE26097.1, 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:OAE26097.1};
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 -!- SIMILARITY: Belongs to the AHA1 family.
CC {ECO:0000256|ARBA:ARBA00006817}.
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:OAE26097.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LVLJ01002256; OAE26097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VZB0; -.
DR OrthoDB; 5473696at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR CDD; cd08892; SRPBCC_Aha1; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 3.15.10.20; Activator of Hsp90 ATPase Aha1, N-terminal domain; 1.
DR InterPro; IPR036338; Aha1.
DR InterPro; IPR015310; AHSA1-like_N.
DR InterPro; IPR013538; ASHA1-like_C.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR13009; HEAT SHOCK PROTEIN 90 HSP90 CO-CHAPERONE AHA-1; 1.
DR PANTHER; PTHR13009:SF8; LD43819P; 1.
DR Pfam; PF09229; Aha1_N; 1.
DR Pfam; PF08327; AHSA1; 1.
DR SMART; SM01000; Aha1_N; 1.
DR SUPFAM; SSF103111; Activator of Hsp90 ATPase, Aha1; 1.
DR SUPFAM; SSF55961; Bet v1-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 29..165
FT /note="Activator of Hsp90 ATPase AHSA1-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM01000"
SQ SEQUENCE 350 AA; 39068 MW; CF0C0A6A4444CFFA CRC64;
MAKFGEGDKR WIVEDRKDGA NVHNWHWSEK DCMEWSKKRL EELLNNVPIL SGEGGLWIST
TTVESVAGEA YVNIRKGKII PGYELKVRVS WVGEAKDGSG TVLSKVEGKV EFPYIADENA
DEEPEVKILV LDETPIGQRM KDAFHAKGKS IVLARVLTYV KEIAAGGPAK DELEGKGTPL
KGAVGKGKSV LSGKDVVVEK AVVPPKNKLK EGFKTISIVE KFHCRPRDLY TTLLDENRWK
GFTQSKATIS KEVGGSFTLF DGAIAGVNEE LQEDKLIRQK WRFNNWADGH FSHVSLTFEE
PEIGLTVVKL THTDVPEEDR YGNATVVENT EKGWRDLIFH KIRAVFGYGI
//