ID A0A0F7NG93_9ACTN Unreviewed; 830 AA.
AC A0A0F7NG93;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:AKH85762.1};
GN ORFNames=AA958_30060 {ECO:0000313|EMBL:AKH85762.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH85762.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH85762.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH85762.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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DR EMBL; CP011492; AKH85762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7NG93; -.
DR STRING; 444103.AA958_30060; -.
DR KEGG; strc:AA958_30060; -.
DR PATRIC; fig|444103.5.peg.6347; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000034283; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10170; HSP70_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
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; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283}.
FT COILED 638..682
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 830 AA; 89737 MW; DE63E9ADDB4BBAA4 CRC64;
MRETIDFGID LGTTNSEIAV FANGRPRIIK NNENWDYTPS AVWMPKPGMI HVGRRARERV
EADPHDACAE FKLQMGLEDA AFAFRRAGVS LTPEQLSAEV LKSLRRDAAH DLGEPPAAAV
ITVPASFALN QSNATSKAAE LAGLGKKCPL IHEPNAAALA YGVDNAAESA YWMVFDLGGG
TFDAAVMSKR DGELQLLQHA GDPHLGGKNI DWAIVDDLLA PAVVRDFGLR DFTRGNGQWR
TNFAKLKAAA EAAKIELSRA AEAELFVDLK IDGDEETFSY TLTRGALDDL ALPVYTQAVK
LCREALAQGS LRPDHIDQLL LVGGATLAPG LRELLADPRE GLGISIDHSQ DPTTVVARGA
AIFAGSVRLP APPQRPTAGT FTAELIYEPQ SLDTTGIPVA GKLRSADPVD WTRYSVFLHS
PGGDYQSPQV ALDANGGFYT TVAIEAEATT RFTVELTDAA GVRQKLTPDT LSLTHTRTLP
AGPVLTHSLG IGKYDGTYGP IVRKGATLPV HGSNKYRTTI ALTRTDPDAV IRIPLLEGEE
PDAKNNKEVG EVSFRRGDLR YDLPEGSEVE VTYEVGTIGQ AKAIVETMDT EFEADVRLQG
AQPEHGELVA GLHRLEQRLP ELGVRARESG SPGADAVLRE VSEDMGRLRK QVDNAVADPG
AALECDQRLR KLHAQLDDVE RDSIEIPRLM LELGDALKEC EGLLRRGGGA AERQELERLR
GLVNRAMQGG GQRVAELERL LTQTRELYVE ILNSTGQLEY KIFEELAGSR GLMEPRAKAE
AALAEGERAY AARDRFALGD VNRRLYAMLP AHARGAHADK AAARGNGGLR
//
