ID A0A061H9V4_9BASI Unreviewed; 669 AA.
AC A0A061H9V4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPQ29672.1};
GN ORFNames=PFL1_02892 {ECO:0000313|EMBL:EPQ29672.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ29672.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ29672.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ29672.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; KE361630; EPQ29672.1; -; Genomic_DNA.
DR RefSeq; XP_007878596.1; XM_007880405.1.
DR AlphaFoldDB; A0A061H9V4; -.
DR GeneID; 19317005; -.
DR KEGG; pfp:PFL1_02892; -.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000053664; 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 GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd11733; HSPA9-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
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 NCBIfam; TIGR02350; prok_dnaK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 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:UP000053664}.
FT REGION 649..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 71761 MW; 4DFE35BFAAEA99EB CRC64;
MISQSLRAAA PATRMLNQPL RSAPSMARLA PMGARFNSGK VSGPVIGIDL GTTNSCVSVM
EGQQARVIEN SEGGRTTPSV VAFTKDGERL VGLPAKRQAV VNPEATLFAT KRLIGRKFQD
KEVQKDLSNV PFKIVPHSNG DAWLEARGQK YSPSQIGAFV VGKMKDTASG YLGKPVKHAV
ITVPAYFNDS QRQATKDAGA IAGLDVLRVI NEPTAAALAY GMDRDDSSVI AVFDLGGGTF
DISILEMQKG VFEVKSTNGD THLGGEDFDI VLVEHLVNEF KKESNIDLSK DRMAIQRIRE
AAEKAKIELS STSQTDISLP YITADASGPK HINTKLTRAQ LEGLVGKLVD RTVEPCKKAL
SDAGVKPSEI QDVIMVGGMS RMPKVLETVK SIFNRDPSKG VNPDEAVAIG ASIQGGVLSG
QVTDVLLLDV TPLSLGIQTL GGVFTRLINR NTTIPTKKSQ VFSTAADGQT AVDIQVYQGE
RELVRDNKLL GNFQLTGIPP APKGVPQIEV TFDIDADGIM HVSASDKATN KDQSMTISAG
SGLSDTEIER MVADAEQYAE SDKARKAVIE EANRAHSVCG ETTKAMQEFS EQLPADEKEK
LNVLIKETEE LAAKGLNADS DVTADAIREK IDATQQASLQ LFKLVYEKRG QQGSSEEAKP
AEGEGEKKQ
//
