ID Q5KPD7_CRYNJ Unreviewed; 614 AA.
AC Q5KPD7;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN OrderedLocusNames=CNA03160 {ECO:0000313|EMBL:AAW40938.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW40938.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW40938.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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; AE017341; AAW40938.1; -; Genomic_DNA.
DR RefSeq; XP_566757.1; XM_566757.1.
DR AlphaFoldDB; Q5KPD7; -.
DR SMR; Q5KPD7; -.
DR STRING; 214684.Q5KPD7; -.
DR PaxDb; 214684-Q5KPD7; -.
DR EnsemblFungi; AAW40938; AAW40938; CNA03160.
DR GeneID; 3253387; -.
DR KEGG; cne:CNA03160; -.
DR VEuPathDB; FungiDB:CNA03160; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_0_1_1; -.
DR InParanoid; Q5KPD7; -.
DR OMA; HQTTVQF; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000002149; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd10233; HSPA1-2_6-8-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF467; RIBOSOME-ASSOCIATED MOLECULAR CHAPERONE SSB1-RELATED; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW Stress response {ECO:0000313|EMBL:AAW40938.1}.
FT COILED 571..598
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 614 AA; 67127 MW; 89E440DC463A98FF CRC64;
MSAEDVFEGA IGIDLGTTYS CVGVWQNDRV EIIANDQGNR TTPSYVAFTE GERLIGDAAK
NQSAMNPLNT IFDAKRLIGR RYDDADVKKD MKHWPFSVID KDGSPYVEVD YLNEKKTFSP
QEISAMVLTK MKEIAEAKIG KTVKKAVVTV PAYFNDSQRL ATKDAGAIAG LEVLRIINEP
TAAAIAYGLD EKTEEERNVL IFDLGGGTFD VSLLTIQGKV FSVKATAGDT HLGGEDFDNN
LLEHFKAEFK RKTKLDISDD ARALRRLRSA CERAKRTLSS VTQTTVEVDS LYQGNDFSSN
ITRARFEEIN AVAFKSTVDP VEKVLKDSKI PAAKVDDIVL VGGSTRIPKI QSLVSEYFGG
RQLNKSINPD EAVAYGAAVQ AAVLTGQTSD KTADLLLLDV APLSLGVAMQ GDVFGVVLPR
NTPIPSNKSR VFTTVEDNQT TVMFPVYEGE RTQCKDNRLL GEFELSGIPP MPRGQAELVC
TFEVDANGLL KVSAQDRASG RKAQITIQNS VGRLSSEEIQ AMIKDAEQFK NADKDFSARH
EAKSDLEAYL HTCEQSISAP ELSMKIKRGA RAAVESEIAK ALEKLEQEDA TADELKKAQL
GVKRAMQKAM ASAR
//
