HSP60_EMENI
ID HSP60_EMENI Reviewed; 588 AA.
AC Q5B041; C8V2L8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Heat shock protein 60;
DE AltName: Full=60 kDa chaperonin;
DE AltName: Full=Protein Cpn60;
DE Flags: Precursor;
GN Name=hsp60; ORFNames=AN6089;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17258477; DOI=10.1016/j.fgb.2006.12.001;
RA Kim Y., Nandakumar M.P., Marten M.R.;
RT "Proteome map of Aspergillus nidulans during osmoadaptation.";
RL Fungal Genet. Biol. 44:886-895(2007).
CC -!- FUNCTION: May participate in assembly and/or disassembly of proteins
CC imported into the mitochondrion. HSP60 are ATPases and have affinity
CC for unfolded proteins (By similarity). Involved in osmoadaptation.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- INDUCTION: Up-regulated when grown with elevated levels of potassium
CC chloride. {ECO:0000269|PubMed:17258477}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; AACD01000104; EAA58064.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF70208.1; -; Genomic_DNA.
DR RefSeq; XP_663693.1; XM_658601.1.
DR AlphaFoldDB; Q5B041; -.
DR SMR; Q5B041; -.
DR STRING; 162425.CADANIAP00006926; -.
DR PRIDE; Q5B041; -.
DR EnsemblFungi; CBF70208; CBF70208; ANIA_06089.
DR EnsemblFungi; EAA58064; EAA58064; AN6089.2.
DR GeneID; 2870917; -.
DR KEGG; ani:AN6089.2; -.
DR VEuPathDB; FungiDB:AN6089; -.
DR eggNOG; KOG0356; Eukaryota.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; Q5B041; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 415781at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0006458; P:'de novo' protein folding; IEA:EnsemblFungi.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0071470; P:cellular response to osmotic stress; IEP:AspGD.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:EnsemblFungi.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; IEA:EnsemblFungi.
DR GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR GO; GO:0050821; P:protein stabilization; IEA:EnsemblFungi.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..588
FT /note="Heat shock protein 60"
FT /id="PRO_0000348279"
SQ SEQUENCE 588 AA; 61847 MW; 2FCB3E02402FF3D1 CRC64;
MQRALSSRTS VLSAASKRAA FTKPAGLNLQ QQRFAHKELK FGVEARAQLL KGVDTLAKAV
TSTLGPKGRN VLIESPYGSP KITKDGVTVA KAVQLQDKFE NLGARLLQDV ASKTNELAGD
GTTTATVLAR AIFSETVKNV AAGCNPMDLR RGIQAAVEAA VDYLQQNKRD ITTGEEIAQV
ATISANGDTH VGKLISTAME RVGKEGVITV KEGKTLEDEL EVTEGMRFDR GYTSPYFITD
AKAQKVEFEK PLILLSEKKI SAVQDIIPAL EASTTLRRPL VIIAEDIEGE ALAVCILNKL
RGQLQVAAVK APGFGDNRKS ILGDLGVLTN GTVFTDELDI KLEKLTPDML GSTGSITITK
EDTIILNGEG SKDAIAQRCE QIRGVMADPT TSEYEKEKLQ ERLAKLSGGV AVIKVGGASE
VEVGEKKDRV VDALNATRAA VEEGILPGGG TALLKAAANG LENVKPANFD QQLGVSIVKS
AITRPARTIV ENAGLEGSVI VGKLTDEFSK DFNRGFDSAK GEYVDMIAAG IVDPLKVVRT
ALVDASGVSS LLGTTEVAIV EAPEEKGPAA PGGMGGMGGM GGMGGGMF
