ID A0A0K9PRZ7_ZOSMR Unreviewed; 366 AA.
AC A0A0K9PRZ7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Activator of 90 kDa heat shock protein ATPase {ECO:0000313|EMBL:KMZ71719.1};
GN ORFNames=ZOSMA_177G00470 {ECO:0000313|EMBL:KMZ71719.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ71719.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:KMZ71719.1}.
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DR EMBL; LFYR01000664; KMZ71719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PRZ7; -.
DR STRING; 29655.A0A0K9PRZ7; -.
DR OMA; CEVNQRK; -.
DR OrthoDB; 5473696at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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:UP000036987};
KW Stress response {ECO:0000313|EMBL:KMZ71719.1}.
FT DOMAIN 29..168
FT /note="Activator of Hsp90 ATPase AHSA1-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM01000"
FT REGION 170..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 41391 MW; B17D3F71638C64B2 CRC64;
MAKYGEGDKR WIVEDRPDGA NVHNWHWSER DCMEWSRNMF SSLFRSLPIL TGEGGLSIQT
KTVDKVQGEA YVNIRKGKII PGYELCLSIS WEAEILPSDP SSGPIAKVNG TVEIPYLADE
NADEDPELRI TVRDDDGPVG KRVKDAFFTK GKPVILEKIK EFVKAMAQGG PARDDVDAKK
PKSQQQQQQK QNIAGDASGN SGIARKVDVE KKKLPQMTNS PPKKKNDGFK SIVLTERFNC
RAKDMYEILM DENRWKGFTQ SNARIQKEVG GSFSIFNESV TGTIVELKES KLIVQKWRFS
SWADEVYSIV RMEFDEPESG LTIIKLTQVN VPIEDRFGNS TVVENTEKGW KDLIFQRIRN
VFGFGM
//
