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
//