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Database: UniProt
Entry: A0A067LXZ5_9AGAM
LinkDB: A0A067LXZ5_9AGAM
Original site: A0A067LXZ5_9AGAM 
ID   A0A067LXZ5_9AGAM        Unreviewed;       389 AA.
AC   A0A067LXZ5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE            EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN   ORFNames=BOTBODRAFT_180898 {ECO:0000313|EMBL:KDQ07230.1};
OS   Botryobasidium botryosum FD-172 SS1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Botryobasidiaceae; Botryobasidium.
OX   NCBI_TaxID=930990 {ECO:0000313|EMBL:KDQ07230.1, ECO:0000313|Proteomes:UP000027195};
RN   [1] {ECO:0000313|Proteomes:UP000027195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-172 SS1 {ECO:0000313|Proteomes:UP000027195};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00001629};
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DR   EMBL; KL198112; KDQ07230.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067LXZ5; -.
DR   STRING; 930990.A0A067LXZ5; -.
DR   HOGENOM; CLU_709777_0_0_1; -.
DR   InParanoid; A0A067LXZ5; -.
DR   Proteomes; UP000027195; 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   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; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00329; HSP70_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027195}.
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   389 AA;  42396 MW;  4298DAFC8A72F3DD CRC64;
     MQASKHPSTI ARSPATTRPR TRPNTPRLTM DSYTIARPTT PTHDLPDAAP DDLIEDAFGS
     PQSLTSTLVG DDDGDLAAAF AANEAEVATF VADAAGELAP NVNPTLFGHD GSIVAAPIPF
     SAIPGFEEAV GDEVERLEAL LPDHATSFDM DAVRVLARAR VREIVAQLLR GNEYVDEGED
     NEDAVEEGFA ARDNIGEEEA ASGEDGIQRR RQKRIPPNPE NIVFDAKRLV GHKMSDADIT
     HDQKHWPFKV VDKSGKPSIQ VKHKGETKDF TPEAYLGKKA TKDAGTIVGL IILRIVIEPT
     ARAIANSLDK KDGERQIIYD LGGGTFDVSL MSSRYWLLLV TPILVEDFDN RVIDYFVKLY
     KKKTGIGVGR NLCVPQARGR GGQSYVRTL
//
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