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Database: UniProt
Entry: K5WX27_PHACS
LinkDB: K5WX27_PHACS
Original site: K5WX27_PHACS 
ID   K5WX27_PHACS            Unreviewed;       338 AA.
AC   K5WX27;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   03-MAY-2023, entry version 33.
DE   RecName: Full=Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein {ECO:0000259|SMART:SM01000};
GN   ORFNames=PHACADRAFT_255354 {ECO:0000313|EMBL:EKM55032.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM55032.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM55032.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM55032.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
CC   -!- SIMILARITY: Belongs to the AHA1 family.
CC       {ECO:0000256|ARBA:ARBA00006817}.
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DR   EMBL; JH930472; EKM55032.1; -; Genomic_DNA.
DR   RefSeq; XP_007395379.1; XM_007395317.1.
DR   AlphaFoldDB; K5WX27; -.
DR   STRING; 650164.K5WX27; -.
DR   GeneID; 18916282; -.
DR   KEGG; pco:PHACADRAFT_255354; -.
DR   HOGENOM; CLU_049046_1_0_1; -.
DR   InParanoid; K5WX27; -.
DR   OrthoDB; 5473696at2759; -.
DR   Proteomes; UP000008370; 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:SF22; 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:UP000008370}.
FT   DOMAIN          19..157
FT                   /note="Activator of Hsp90 ATPase AHSA1-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01000"
FT   REGION          162..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   338 AA;  36537 MW;  7A09B26F68796A5D CRC64;
     MATVPPPMAV STANWHWKNK NVTPWAKNWF ERELTTVSVK GDGEEEVFVS EVAEVDGDVE
     LGQRKSKLLT IYDCKVELKW TGKTADGTEV LGKLTIPEVS HEITLDGISE YQWHWSLSTA
     RSPAVDKVFE LAKARLPTAL ETKLSEFPSA IINTHGKDLT ISAEPSRQST PAPSNIAPSA
     AASATSSSAA ATAKPAVKKD AKAVNSTTVS VDSTFMASAE DLFSILTNEN RIPSWTRAPA
     KSTAQPDTEY FLFGGGVKGK YVSLNSPKEI IQTWALSSPT WPDGHFATLT TTLDQGSDHT
     KVTWSLAGVP LGMEDEINRN INGYYVHGLK SIGLGSEL
//
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