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Database: UniProt
Entry: A0A423TI28_PENVA
LinkDB: A0A423TI28_PENVA
Original site: A0A423TI28_PENVA 
ID   A0A423TI28_PENVA        Unreviewed;       509 AA.
AC   A0A423TI28;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Heat shock protein 83 {ECO:0000256|ARBA:ARBA00021845};
GN   ORFNames=C7M84_005287 {ECO:0000313|EMBL:ROT76136.1};
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT76136.1, ECO:0000313|Proteomes:UP000283509};
RN   [1] {ECO:0000313|EMBL:ROT76136.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT76136.1};
RA   Zhang X., Yuan J., Li F., Xiang J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ROT76136.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT76136.1};
RA   Sun Y., Gao Y., Yu Y.;
RT   "The decoding of complex shrimp genome reveals the adaptation for benthos
RT   swimmer, frequently molting mechanism and breeding impact on genome.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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:ROT76136.1}.
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DR   EMBL; QCYY01001690; ROT76136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423TI28; -.
DR   STRING; 6689.A0A423TI28; -.
DR   EnsemblMetazoa; XM_027357149.1; XP_027212950.1; LOC113806043.
DR   Proteomes; UP000283509; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
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:SF34; HEAT SHOCK PROTEIN 83; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 2.
DR   PIRSF; PIRSF002583; Hsp90; 2.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
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.
DR   PROSITE; PS00298; HSP90; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW   Stress response {ECO:0000313|EMBL:ROT76136.1}.
FT   DOMAIN          33..187
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
SQ   SEQUENCE   509 AA;  59138 MW;  32F7FA20A67839F5 CRC64;
     MVEETMSEEV ETFAFQAEIA QLMSLIINTF YSNKEIFLRE LISNSSDALD KIRYESLTDP
     SKIESGKDLF IKLVPNKDDR TLTIIDSGIG MTKADLVNNL GTIAKSGTKA FMEALQAGAD
     ISMIGQFGVG FYSAYLVADK VTVVSKNNDD EQYIWESSAG GSFTVRHDTG EPIGRGTKIT
     LHLKEDQTEY LEERRVKEIV KKHSQFIGYP IKLLVEKERD KTKPLWTRNP DDISKEEYGE
     FYKSLTNDWE DHLAVKHFSV EGQLEFRALL FLPRRAPFDL FENRKQKNKI KLYVRRVFIM
     ENCEELIPEY LNFINGVVDS EDLPLNISRE MLQQNKILKV IRKNLVKKTL ELFEEIVDDK
     ESYKKFYENF SKNLKLGIHE DSTNRKKLAE FLRYHTSASG DEMSSLKEYI SRMKENQKVI
     YYITGETREQ VQNSAFVERV KKRGFEVIYM TEPIDEYCVQ QLKEYDGKQL VSVMKDILDK
     RVEKVVVSNR LVTSPVHRDR RPWATPRST
//
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