ID A0A1V6URU9_9EURO Unreviewed; 711 AA.
AC A0A1V6URU9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQE41130.1};
GN ORFNames=PENCOP_c005G08155 {ECO:0000313|EMBL:OQE41130.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE41130.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE41130.1}.
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DR EMBL; MDDG01000005; OQE41130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6URU9; -.
DR STRING; 36646.A0A1V6URU9; -.
DR OrthoDB; 276440at2759; -.
DR Proteomes; UP000191500; 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; cd10228; HSPA4_like_NDB; 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; PTHR45639:SF4; HSC70CB, ISOFORM G; 1.
DR PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 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; PS01036; HSP70_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500}.
FT REGION 504..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 79446 MW; 75EE6F965A59BB92 CRC64;
MSVVGIDLGA QSTKIGVARN KGIDIIANEV SNRQTPSVVG FTPRSRNLGE AAKGAEISNL
KNTVSSLKRL IGRSFNDPDV AIEQEYNTCT LVDVDGQAGV EVNYLGKKEK FTATQLVASY
LSKIKDITAK ELRAPVSDVT VSVPAWFTDV QRRAMLDAGD IAGLNILRLI NDTTATALGY
GITKLDLPGP EEKPRRVMFV DIGYSDYTAS IVEFRKGELN VKATAYDRHF GGRNFDKALT
EHLAVEFKEK FKVDIHTNGK AWTRTLVAAE KLKKVLSANA AAPLSVESLM DDTDVRAMVK
REELELMVKP LLDRLTAPLE QALSEAKLQI EDIDHIEMVG GCTRVPAIKE TISKFFGKNL
SFTLNQDEAI ARGCAFSCAT LSPAFRVRDF AVHDIVNYPI DFTWEQSPEI PDEDTSLTVF
SRGNVMPSTK ILTFYRKQPF DLEARYSNVD AMPGKVNPWI GRFSVKGVQA DANNDFMICK
LKARLNLHGI LNVESGYYVE DMEVEEPVEE EKKEGDMDTD SKEEQPKKTR KVKKQVRKGD
LPIVSVTGGF PQDLKEAWTE RENAMYMEDK LVAETDEKKN ELEASIYELR DKIDGVYSEF
ASEEEKEKLK SKLMDTEDWL YEDGEDATKS IYVAKMDDIR FIAGPIIQRY KEKVEAERDA
VRKADEEAAA KRRAEIEAKK AEENANKTEG DAEMKDAPAE GEAQGETEEK Q
//
