ID S7ZFK7_PENO1 Unreviewed; 635 AA.
AC S7ZFK7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Heat shock protein 70 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PDE_02379 {ECO:0000313|EMBL:EPS27436.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS27436.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS27436.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; KB644410; EPS27436.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZFK7; -.
DR STRING; 933388.S7ZFK7; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR OrthoDB; 143at2759; -.
DR PhylomeDB; S7ZFK7; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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:SF395; HEAT SHOCK 70 KDA PROTEIN COGNATE 1-RELATED; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT REGION 605..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 69516 MW; DA335185E1E1F891 CRC64;
MAPAVGIDLG TTYSCVGVFR DDRIEIIAND QGNRTTPSFV AFTDTERLIG DAAKNQVAMN
PHNTVFDAKR LIGRRFEDAE VQADMKHWPF KVVEKATKPI IEVEFKGESK QFTPEEISAM
ILVKMRETAE AYLGGTVNNA VITVPAYFND SQRQATKDAG LIAGLNVLRI INEPTAAAIA
YGLDKKVEGE RNVLIFDLGG GTFDVSLLTI EEGIFEVKST AGDTHLGGED FDNRLVNHFV
NEFKRKHKKD LTTNARALRR LRTACERAKR TLSSAAQTSI EIDSLFEGID FYTSITRARF
EELCQDLFRS TMEPVERVLR DAKIDKASVH EIVLVGGSTR IPKIQKLVSD FFNKDANKSI
NPDEAVAYGA AVQAAILSGD TSSKSTNEIL LLDVAPLSLG IETAGGVMTP LIKRNTTIPT
KKSETFSTYS DNQPGVLIQV FEGERARTKD NNLLGKFELT GIPPAPRGVP QIEVVFDLDA
NGIMNVSAVE KGTGKTNKIT ITNDKGRLSK EEIERMLSEA EKYKAEDEAE AGRIQAKNGL
ESYAYSLKNT LSEGKLQISE DDKKKVEDKI NEVISWLDNN QTAEKDEYES QQKELEGVAN
PIISAAYGGA APGGAPGGAA PRPADDVEEK PEELD
//
