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Database: UniProt
Entry: A0A178EE25_9PLEO
LinkDB: A0A178EE25_9PLEO
Original site: A0A178EE25_9PLEO 
ID   A0A178EE25_9PLEO        Unreviewed;       330 AA.
AC   A0A178EE25;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Aha1domain family protein {ECO:0000313|EMBL:OAL53905.1};
GN   ORFNames=IQ07DRAFT_609130 {ECO:0000313|EMBL:OAL53905.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL53905.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL53905.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL53905.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AHA1 family.
CC       {ECO:0000256|ARBA:ARBA00006817}.
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DR   EMBL; KV441639; OAL53905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EE25; -.
DR   STRING; 765867.A0A178EE25; -.
DR   InParanoid; A0A178EE25; -.
DR   OrthoDB; 5473696at2759; -.
DR   Proteomes; UP000077535; 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:UP000077535}.
FT   DOMAIN          13..146
FT                   /note="Activator of Hsp90 ATPase AHSA1-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01000"
FT   REGION          146..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   330 AA;  36242 MW;  4F24D2C98F0BEF69 CRC64;
     MVLHNPNNWH WVNKDVSGWA REYLDQTLPQ LSSEQDGVTA KIDKVVSMDG DVDVSQRKGK
     VITIFDVKLK LEYSGKNTEG EEASGTITIP EVAHDTEEDE YVFDIDVYSD ESSKQPVKDL
     VRSKLVPQLR TSLAKLGPAL MAEHGKDIQH APGSNPSSGF TTPKVYSSSS VNKASGPTSG
     AASSQKSGSG AVVNVTTITD STEFRTDAAN LFQTFTDPQR IAAFTRSPPK NFTGAKPGGT
     FELFGGNVSG EFTELEEPTH IVQKWRLAQW PAGHYSTLSI WFDQNDVDAV TVMRVEWKGV
     PVGQEEPTKT NWDQYYVRSI KTTFGFGTVL
//
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