GenomeNet

Database: UniProt
Entry: F1LAX9_ASCSU
LinkDB: F1LAX9_ASCSU
Original site: F1LAX9_ASCSU 
ID   F1LAX9_ASCSU            Unreviewed;       375 AA.
AC   F1LAX9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Heat shock protein 90 {ECO:0000313|EMBL:ADY47283.1};
DE   Flags: Fragment;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY47283.1};
RN   [1] {ECO:0000313|EMBL:ADY47283.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JI175899; ADY47283.1; -; mRNA.
DR   AlphaFoldDB; F1LAX9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   2: Evidence at transcript level;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Stress response {ECO:0000313|EMBL:ADY47283.1}.
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         375
FT                   /evidence="ECO:0000313|EMBL:ADY47283.1"
SQ   SEQUENCE   375 AA;  44263 MW;  1BD1F2270C0ED930 CRC64;
     MRVRRKKEGE IEDIGEDEEE DKKDKEKDKK KKKKIKEKYH EDEELNKTKP IWTRNPDDIS
     NEEYAEFYKS LSNDWEDHLA VKHFSVEGQL EFRALLFVPQ RAPFDLFENK KTKNAIKLYV
     RRVFIMENCD ELMPEYLNFI KGVVDSEDLP LNISREMLQQ SKILKVIRKN LVKKCLELFD
     EIAEDKDNFK KFYEQFSKNI KLGIHEDSTN RKKLAEFLRF YTSNSPEEMC SLKDYVGRMK
     ENQKQIYFIT GESKESVASS AFVERVKRRG FEVIYMTDPI DEYCVQQLKE YDGKKLVSVT
     KEGLELPESE EEKKKFEEDK VKYENLCKVI KDILEKKVEK VVVSNRLVSS PCCIVTSGIW
     LVSKHGTHHE GASTP
//
DBGET integrated database retrieval system