ID C1G445_PARBD Unreviewed; 323 AA.
AC C1G445;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein {ECO:0000259|SMART:SM01000};
GN ORFNames=PADG_01711 {ECO:0000313|EMBL:EEH45561.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH45561.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH45561.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH45561.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SIMILARITY: Belongs to the AHA1 family.
CC {ECO:0000256|ARBA:ARBA00006817}.
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DR EMBL; KN275958; EEH45561.2; -; Genomic_DNA.
DR RefSeq; XP_010757039.1; XM_010758737.1.
DR AlphaFoldDB; C1G445; -.
DR STRING; 502780.C1G445; -.
DR GeneID; 22581326; -.
DR KEGG; pbn:PADG_01711; -.
DR VEuPathDB; FungiDB:PADG_01711; -.
DR eggNOG; KOG2936; Eukaryota.
DR HOGENOM; CLU_049046_1_0_1; -.
DR InParanoid; C1G445; -.
DR OMA; CEVNQRK; -.
DR OrthoDB; 5473696at2759; -.
DR Proteomes; UP000001628; 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:UP000001628}.
FT DOMAIN 13..146
FT /note="Activator of Hsp90 ATPase AHSA1-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM01000"
FT REGION 147..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 36027 MW; 4C006093A05EFAC5 CRC64;
MVLHNPNNWH WVNKDAFAWT KDYLQKTLST ISAEENGVTA QIKRVISMDG DVDVSQRKGK
VITLFDVKLQ LEYEGKTSDD EEVSGSINIP EVAHDTEEDQ YVFDIGIYSE SASKQPVKDL
VRSKLVPEMR KELAKLGAAL ITEHGKDIQH APESNPSSGF ATPAHLPKTT TPAPSTSTPS
STTTGAGTVN TTTVTATDEF RTTAEELYTT FTDPQRIAAF TRGAPRRFDG AKAGGKFSIF
DGNVEGEYVK IEPSTNIVQK WRLAQWPEGH YSTLEIKFDQ NDVDKVTNMR VQWEGVPVGQ
EEVVKRNWEG YYVRSIKQTF GYV
//
