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Database: UniProt
Entry: F8Q855_SERL3
LinkDB: F8Q855_SERL3
Original site: F8Q855_SERL3 
ID   F8Q855_SERL3            Unreviewed;       316 AA.
AC   F8Q855;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein {ECO:0000259|SMART:SM01000};
GN   ORFNames=SERLA73DRAFT_60426 {ECO:0000313|EMBL:EGN95743.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
CC   -!- SIMILARITY: Belongs to the AHA1 family.
CC       {ECO:0000256|ARBA:ARBA00006817}.
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DR   EMBL; GL945485; EGN95743.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8Q855; -.
DR   STRING; 936435.F8Q855; -.
DR   HOGENOM; CLU_049046_1_0_1; -.
DR   InParanoid; F8Q855; -.
DR   OMA; CEVNQRK; -.
DR   OrthoDB; 5473696at2759; -.
DR   Proteomes; UP000008063; 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:UP000008063}.
FT   DOMAIN          12..151
FT                   /note="Activator of Hsp90 ATPase AHSA1-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01000"
FT   REGION          156..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   316 AA;  34016 MW;  261907114CF6CAA0 CRC64;
     MPASTANWHW KNKNVTPWAK TWFERELTSV TIQGDGSEEK VSITSVIEVD GDVELGQRKS
     KLITIYDCRI DLDWSGTASD GTEVNGKVSI PEVSHENTLD GHSDYIYDWS LKTQSSPAVD
     ALYKLARARL PAALEAKFAQ FPVALIDTHG KDLTVSTEAS RTGTPAPSTV PAATSTSTAA
     APVPAPKSVP EKKVALNTSR VKAEARFMAA ADDLFSLLTD EKRIPMWTRA PAQSSAQAGS
     DFSLFGGGVK GKYISLTPPK EIVQSWALQS PTWPSGHSAT LTTTLDQSSD STKITFALDG
     VPSGLEDEIT RNLEGY
//
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