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Database: UniProt
Entry: A0A0L6UT44_9BASI
LinkDB: A0A0L6UT44_9BASI
Original site: A0A0L6UT44_9BASI 
ID   A0A0L6UT44_9BASI        Unreviewed;       705 AA.
AC   A0A0L6UT44;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE            EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN   ORFNames=VP01_386g18 {ECO:0000313|EMBL:KNZ51674.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ51674.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ51674.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ51674.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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:KNZ51674.1}.
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DR   EMBL; LAVV01008912; KNZ51674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6UT44; -.
DR   STRING; 27349.A0A0L6UT44; -.
DR   VEuPathDB; FungiDB:VP01_386g18; -.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000037035; 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; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF467; RIBOSOME-ASSOCIATED MOLECULAR CHAPERONE SSB1-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; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037035}.
SQ   SEQUENCE   705 AA;  76612 MW;  E87FE166820F1BCF CRC64;
     MSPASTISVK ATYTSVLGSF LATFQAVNLT PTCFGIVFGL FTWVSVACHD FTYSRGIALF
     ARNTSRRSAE QNPTVDGNVP GADAESTEFN GAIGIDLGTT YSCVGVWQND RVEIIANDQG
     NRTTPSYVAF TSEERLIGDA AKNQAAMNPR MTVFDAKRLI GRRFDDSDVK KDMVHWPFTV
     IEKDGNPFIQ VDYLGETKTF SPQEISAMVL TKLKETAETK LGKEVKKAVI TVPAYFNDSQ
     RLSTKDAGAI AGLDVLRIIN EPTAAAIAYG LGEASDKKEK KERTVLIFDL GGGTFDVSLL
     SIAGGVFTVK ATAGDTHLGG EDFDNALLEH FKSEFKRKTK LDIDGDARAL RRLRSACERA
     KRTLSSVTQT TVEVDSLFQG TDFSSAISRA RFEEINAQTF RSTLDPVDKV LKDAKIDKSK
     VEDIVLVGGS TRIPKIQSLV SDFFGGRQLN KSINPDEAVA YGAAVQAAVL TGQTSEKTAD
     LLLLDVAPLS LGVAMQGDVF GVVVPRNTPI PTNKSRTFTT VEDNQSTVTF PVYEGERVTC
     KENRLLGEFE MAFQLSGITP QPRGQAELVC TFEVDANGLL KVSACDRTSG RRANITITNS
     VGRLSSAEID QMIKDAESFK QADKEFSAKH EAKQELESYI SQVEATITSP EVGMKIKRNN
     KAAVEAELAK ALEKLEIEDS SADELKKCQL GLKRAMQKAM AGTAR
//
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