ID A0A0F4YKA3_TALEM Unreviewed; 582 AA.
AC A0A0F4YKA3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=non-chaperonin molecular chaperone ATPase {ECO:0000256|ARBA:ARBA00012554};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
GN ORFNames=T310_8010 {ECO:0000313|EMBL:KKA18038.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA18038.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA18038.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA18038.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-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:KKA18038.1}.
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DR EMBL; LASV01000508; KKA18038.1; -; Genomic_DNA.
DR RefSeq; XP_013324650.1; XM_013469196.1.
DR AlphaFoldDB; A0A0F4YKA3; -.
DR STRING; 1408163.A0A0F4YKA3; -.
DR GeneID; 25320275; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
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 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; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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 Oxidoreductase {ECO:0000313|EMBL:KKA18038.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
SQ SEQUENCE 582 AA; 63265 MW; 653BA7259D739E08 CRC64;
MSDEVYDGAI GIDLVANEQG NFTTPSYVSF TDKERLIGEA AKNQAAMNPK NTIFDIKRLI
GRRFDDPVVK KDIESWPFKV VEQGGNPVVE VEYLGETKIF TPQEISSMVL MKMKEVAETK
LGKKVSKAVI TVPAYFNDNQ RQATKDAGAI AGLNVLRIIN EPTAAAIAYG LGSGKSDKER
NVLIYDLGGG TFDVSLLNIQ GGVFTVKATA GDTHLGGQDF DTNLLEHFKK EFQRKTGKDL
SGDSRALRRL RTACERAKRT LSNATQTTVE IDSLFDGEDF NAQITRARFE DLNAKAFAGT
LEPVQQVLKD AGLDKSNVDE IVLVGGSTRI PRIQKLLSDF FDGKKLEKSI NPDEAVAYGA
AVQAGILSGK ATSAETSDLL LLDVVPLSLG VAMEGNIFAP VVPRGQTVPT IKKRTFTTVV
DNQQTVQFPV YQGERANCDD NTLLGEFTLS PIPPMKAGEA VLEVVFEVDV NGILKVTATE
KSSGRSANIT ISNAVGKLSS TEIEKMISGM CLYLSALFEL RIISLTGDPT MSLKLKRGNK
EKIESALSDA MAQLEIEDST PDDFKKKELA LKRLITKAMA TR
//
