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Database: UniProt
Entry: A0A1Q5T389_9EURO
LinkDB: A0A1Q5T389_9EURO
Original site: A0A1Q5T389_9EURO 
ID   A0A1Q5T389_9EURO        Unreviewed;       798 AA.
AC   A0A1Q5T389;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Heat shock protein 78, mitochondrial {ECO:0000313|EMBL:OKO94595.1};
GN   ORFNames=PENSUB_11862 {ECO:0000313|EMBL:OKO94595.1};
OS   Penicillium subrubescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKO94595.1, ECO:0000313|Proteomes:UP000186955};
RN   [1] {ECO:0000313|EMBL:OKO94595.1, ECO:0000313|Proteomes:UP000186955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 132785 {ECO:0000313|EMBL:OKO94595.1,
RC   ECO:0000313|Proteomes:UP000186955};
RA   De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA   Grigoriev I., Riley R., Granchi Z.;
RT   "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
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:OKO94595.1}.
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DR   EMBL; MNBE01000719; OKO94595.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q5T389; -.
DR   STRING; 1316194.A0A1Q5T389; -.
DR   OrthoDB; 35211at2759; -.
DR   Proteomes; UP000186955; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF176; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW   Stress response {ECO:0000313|EMBL:OKO94595.1}.
FT   DOMAIN          120..264
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          519..661
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          697..786
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          333..413
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   798 AA;  88330 MW;  2C8EBE488F09C256 CRC64;
     MAARLALNSR TRLLRTPNLP TSSRLLSTTT RSAHLPRILA PLLTSAARTT SVTSVRHYAN
     GRPHPPGGTH RMNMSPEPEK PALEQFGVDL TEKAKAGKLD PVIGRDAEIH RTIQVLSRRT
     KNNPVLIGAA GTGKTAVLEG LAQRIVQGDV PESIKNKRVI SLDLGSLIAG AKFRGDFEER
     LKSVLKEVED AEGKVILFID ELHTLLGLGK AEGSIDASNL LKPALSRGEL QCCGATTLNE
     YRLIEKDVAL ARRFQPILVG EPSVASTISI LRGIKNKYEV HHGVRITDGA LVAAATYSNR
     YITDRFLPDK AIDLVDEAAS ALRLQQESKP DAIRELERDI TTIQIELESL RKETDVSSRE
     RRDKLQEDLK IKQDEVGKLT EVWEKEKAEI DTIKRTKEDL EKARFELEQA QREGNFAKAG
     ELRYSTIPGL EAKLPKEGSE QEAEKQSLIH DSVTADDIGN VVSRTTGIPV NKLMAGEVEK
     LIHMEDTLRQ SVRGQDEALA AVANAVRMQR AGLSGENRPL ASFMFLGPTG VGKTELCKKM
     AEFLFSTETA VVRFDMSEFQ EKHTISRLIG SPAGYVGYDD AGQLTEAVRR KPYAVLLFDE
     FEKAHRDISA LLLQVLDEGF LTDAQGHKVD FRNTLIVLTS NLGAEILVGA DPLHAYKDTG
     GAEVPSDIKK AVMDVVQNAY PPEFLNRMDE FIIFKRLSKE ALRDIVDIRL KELQGRLDSR
     RMTLQVDNEI KDWLCEKGYD PKFGARPLNR LIAKEIGNRL ADKIIRGEVT SGQTVRVSLN
     EDKSTLVVSA EGKVEEEA
//
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