ID C5FUG5_ARTOC Unreviewed; 345 AA.
AC C5FUG5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Aha1 family protein {ECO:0000313|EMBL:EEQ33549.1};
GN ORFNames=MCYG_06368 {ECO:0000313|EMBL:EEQ33549.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ33549.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the AHA1 family.
CC {ECO:0000256|ARBA:ARBA00006817}.
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DR EMBL; DS995706; EEQ33549.1; -; Genomic_DNA.
DR RefSeq; XP_002844404.1; XM_002844358.1.
DR AlphaFoldDB; C5FUG5; -.
DR STRING; 554155.C5FUG5; -.
DR GeneID; 9227284; -.
DR VEuPathDB; FungiDB:MCYG_06368; -.
DR eggNOG; KOG2936; Eukaryota.
DR HOGENOM; CLU_049046_1_0_1; -.
DR OMA; CEVNQRK; -.
DR OrthoDB; 5473696at2759; -.
DR Proteomes; UP000002035; 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:UP000002035}.
FT DOMAIN 13..157
FT /note="Activator of Hsp90 ATPase AHSA1-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM01000"
FT REGION 158..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 38107 MW; 5362D78F85C72C24 CRC64;
MVLHNPNNWH WVNKNVTSWA KAYLEENLVG ISAEENGVTA KINKLVRMDG DVDVSQRKGK
VITLFDVKLQ LDYEGTTSEK EDVTGSIKIP EVAHDTEADE YVQFFVTKDD SQQFDTSIYS
ETAKKQPVKD LVRSKIVPQL RAALVKLAPA LIKEHGKDIQ HAPGSNPSSG FSTPTTLKSS
TPQPATKAAD TAATTTTTTT TSTGKSSVNT VSVNASDEFR TTAEQLYTTF TDPERLAAFT
RGAPRRFDGA KVGGQFSIFD GNVDGEYVTL EKPGLIVQKW RLAQWPEGHY STQEIKFVQN
DVDGVTVLNV RWDGVPVGQE DVVKHNWDGY YVRSIKQTFG FGTIL
//
