ID   A0A093T7X4_PHACA        Unreviewed;       672 AA.
AC   A0A093T7X4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Heat shock cognate protein HSP 90-beta {ECO:0000313|EMBL:KFW90634.1};
DE   Flags: Fragment;
GN   ORFNames=N336_08436 {ECO:0000313|EMBL:KFW90634.1};
OS   Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC   Phalacrocorax.
OX   NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW90634.1, ECO:0000313|Proteomes:UP000053238};
RN   [1] {ECO:0000313|EMBL:KFW90634.1, ECO:0000313|Proteomes:UP000053238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW90634.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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DR   EMBL; KL427279; KFW90634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093T7X4; -.
DR   Proteomes; UP000053238; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   CDD; cd16927; HATPase_Hsp90-like; 1.
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   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   PANTHER; PTHR11528:SF79; HEAT SHOCK PROTEIN HSP 90-BETA-RELATED; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053238};
KW   Stress response {ECO:0000313|EMBL:KFW90634.1}.
FT   REGION          169..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..189
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW90634.1"
FT   NON_TER         672
FT                   /evidence="ECO:0000313|EMBL:KFW90634.1"
SQ   SEQUENCE   672 AA;  77207 MW;  08FCAE558284EFD8 CRC64;
     IRYESLTDPS KLDSGKDLKI DIVPNLRDRT LTLVDTGIGM TKADLINNLG TIAKSGAKAF
     MEALQAGADI SMIGQFGVGF YSAYLVAEKV VVITKHNDDE QYAWESSAGG SFTVRTDRDE
     PIGRGTKVIL YLKEDQTEYL EERRVKEVVK KHSQFIGYPI TLYLEKEREK EISDDEAEEE
     KDEKEEEEPA SKDEEKPKIE DVGSDEEEGD KGKKKKTKKM KEKYIDQEEL NKTKPIWTRN
     PDDITQEEYG EFYKSLTNDW EDHLAVKHFS VEGQLEFRAL LFIPRRAPFD LFENKKKKNN
     IKLYVRRVFI MDSCDELIPE YLNFIRGVVD SEDLPLNISR EMLQQSKILK VIRKNIVKKC
     LELFSELAED KESYKKFYEA FSKNLKLGIH EDSNNRKRLS ELLRYHTSQS GDEVTSLSEY
     VSRMKETQKS IYYITGESKE QVANSAFVER VWKRSFEVVY MTEPIDEYCV QQLKEFDGKT
     LVSVTKEGLE LPEDEEEKKK MEESKAKFET LCKLMKEILD KKVEKVTISN RLVSSPCCIV
     TSTYGWTANM ERIMKAQALR DNSTMGYMMA KKHLEINPDH PIVETLRQKA GADKNDKAVK
     DLVVLLFETA LLSSGFSLED PQTHSNRIYR MIKLGLGIDE DDVTAEEPSA AVPDEIPALE
     GGEDASRMEE VD
//