ID   A0A139HFW3_9PEZI        Unreviewed;       924 AA.
AC   A0A139HFW3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein {ECO:0000259|SMART:SM01000};
GN   ORFNames=AC578_6614 {ECO:0000313|EMBL:KXT01361.1};
OS   Pseudocercospora eumusae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT01361.1, ECO:0000313|Proteomes:UP000070133};
RN   [1] {ECO:0000313|EMBL:KXT01361.1, ECO:0000313|Proteomes:UP000070133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT01361.1,
RC   ECO:0000313|Proteomes:UP000070133};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT01361.1}.
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DR   EMBL; LFZN01000056; KXT01361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139HFW3; -.
DR   STRING; 321146.A0A139HFW3; -.
DR   OrthoDB; 5473696at2759; -.
DR   Proteomes; UP000070133; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT   DOMAIN          13..162
FT                   /note="Activator of Hsp90 ATPase AHSA1-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01000"
FT   REGION          79..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          394..435
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        79..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..770
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..890
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   924 AA;  101492 MW;  E1681E021CE3414F CRC64;
     MVLHNPNNWH WVNKDVSAWT QDYLSKEIVG LKAEKNGVNA EVSKVLSMDG DVDVSQRKGK
     VITIFDVRLS LEWTGSVPVK EEHENDDGTK EERDGKKDVS GTITIPEVAH DTGEDEYVFE
     VDIYSSSLDK EPAKELVRNE IIPQLRKHLQ KLAPALIAEH GKDIQHAPGS NPSSGFSTPR
     TLQNSGVNKS SSGATTSATT SSSNGAVVNT TKLSDQQEFR TTAEQLFETF TDPQRIAAFT
     REPPKIFEGA KVGGKFELFG GNVSGSYTKL DKPTHIEQKW RLGQWPAGHY STLKIKFEQN
     DVDAVTVMRV DWDGVPIGQE EPTKRNWDQY YVRSIKTTFG FGWQLAVAKT RNPTAAHDRL
     HTHTPTPSPT PQTLRYAMDS VAVNRLVQEL SAGFGALQDE YQKLYGQHQA LERKLANARE
     QYNKLAKLYN SEQTATPPLS LTSSPAQPSQ DVFAPRTVAE ILDTRPDTHS KDAANKVRSA
     ISAVQQLRSG LPLDTAAHGV KIWSGPSADR PEGSSSMMPS ISESPLEQDF TVEGKPSQLG
     CPFAGMAKKK KLSSHAASVL SRYERNAANG SVAASTPVSQ TSYVNGRDSF WRRGSRRASF
     VDPIKAEICG LSDHNSASPA AEKALSKGPE QPQIENAELG VCPIRFLDQH SPEEVATYFE
     KHKNELPRSH EMCILRYQSN EEQIKQLDAK YGNLVSMIQG LGQRHKEMLP EDPDPEEQDE
     ERHDDAVSDE KIRKWASSVS AQAPQAADVD EDEGEDRLPH FERPVREIRV GESPSRPWGI
     PVPARYYDKA ESKSSSQPVQ VNSPALQSAK QQGPEIKADP KPAGKCPFDH KALQAMGMTR
     PQPAHPAPQE PGNGAQNPEP APAAEPATDK ETSKPQLGPD ASTHKASATA SPHIVINGPL
     FIGYSPEDAI RILRESGLKV SSED
//