ID M7TRC5_BOTF1 Unreviewed; 909 AA.
AC M7TRC5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN ORFNames=BcDW1_7566 {ECO:0000313|EMBL:EMR83825.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR83825.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KB707979; EMR83825.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TRC5; -.
DR STRING; 1290391.M7TRC5; -.
DR HOGENOM; CLU_005965_0_1_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF467; RIBOSOME-ASSOCIATED MOLECULAR CHAPERONE SSB1-RELATED; 1.
DR Pfam; PF00012; HSP70; 2.
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; 2.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 703..732
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 660..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 99718 MW; 27A182FAFBE5E604 CRC64;
MADEVYEGAI GIDLVANEQG SFTTPSFVSF TDKERLIGES AKNNAAMNPK NTIFDIKRLI
GRRFDDPHTT KDIQSWPFTV VDKDGSPFVQ VEYLGEEKTF SPQEISSMMK EIAEVKLGKK
VEKAVITVPA YFNDNQRQAT KDAGAIAGLN VLRIINEPTA AAIAYGLGAG KSNKERNVLI
YDLGGGTFDV SLLNIQGGVF TVKATAGDTH LGGQDFDTNL LDHFKKEFTR KTKKDLSNDP
RALRRLRTAC ERAKRTLSNG ASTNVEIDSL FDGEDFNAQI TRARFEDLNA KAFSGTLDPV
AQVLKDANID KSKVDEIVLV GGSTRIPKIQ KLLSEFFDNK KLEKSINPDE AVAYGAAVQA
GILSGKATSA ETADLLLLDV VPLSLGVAME GNIFAPVVTR GQTVPPPLGV KTVVIMSSLF
PLVETLLELL VLIVWTCLSN QKWKNSVFLT VFPDKDALLD VKSATGLSFA PALFGIMQAA
TLTISFFKSL PPVLDMKVWA VYVLVLEKPG FKPSLYCGSG TASVTGVRSR FAKYDNGGAL
PRYVKWAQDN GFSIVHKGLV VWCPIPEPVD RPRVRVLFLA LEATLSFFFW TMKSSTKDYN
MGECCYWARD SFPYGGLCSH SALWEGVEGL ELTPQELSDI AAALKVKNKE RHSAFHKKQL
EENRPAYRSR QNKNSTSFRK KNVDKVHRTN GESATKAKDS GRFSCGTCNF SFKSQSDLNR
HNGKARHLAK VAAASKSVQF PVFQGERVNC EDNTSLGEFT LAPIPPMKAG DAVLEVVFEV
DVNGILKVTA TEKTSGRSAN ITIANSVGKL SSSEIEKMVA DAAEFKSSDD AFSKRFESKQ
QLESYISRVE EIISDPTMSI KFKRGNKEKI ESALSDAMAQ LEIEDSTSDD LKKKELALKR
AVTKAMSTR
//