ID   A0A429EMR4_9ACTN        Unreviewed;       829 AA.
AC   A0A429EMR4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:RSN50596.1};
GN   ORFNames=DMH08_32480 {ECO:0000313|EMBL:RSN50596.1};
OS   Actinomadura sp. WAC 06369.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2203193 {ECO:0000313|EMBL:RSN50596.1, ECO:0000313|Proteomes:UP000288610};
RN   [1] {ECO:0000313|EMBL:RSN50596.1, ECO:0000313|Proteomes:UP000288610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 06369 {ECO:0000313|EMBL:RSN50596.1,
RC   ECO:0000313|Proteomes:UP000288610};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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:RSN50596.1}.
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DR   EMBL; QHJN01000169; RSN50596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429EMR4; -.
DR   Proteomes; UP000288610; 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; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288610}.
FT   REGION          807..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   829 AA;  89960 MW;  0B85D9FD0854118D CRC64;
     MTRTTIDFGI DLGTTNSAIA MLSGVGAEVI KNNVSSDTTP SAVMLDRRGR LQVGMRAKQR
     SEDDPDNTCV EFKLRMGTTG RPKEFPAAGR TMTPEEMSAE VLRSLRHDVV QHHGEEIGAA
     VITVPAAFEL SACDATRRAA ELAGLPYAPL LQEPTAAASA YGFQTDTDNA FWLVYDIGGG
     TFDAAVVNVR DGEFTVVNHC GDNYLGGKLL DWAIVEEVLV PAVAAEFRVD DLRRGNPAQR
     RNMAKLKWAA EAAKIELSRA DEAAITVEIA DAAGEPRDFI YDLTRAEVER LMEPLIVRSV
     NLSRKALAES RLGPGDIEKV LLVGGPTLMP YLRERLADPR EGLGIALDHS QDPLTVVARG
     AAIFAGGQRL DAVDAPPPPA ASGEYAVELE YRPVGPDIEP FVGGRVAGAD TAGCSVEFVN
     PDAKPPWRSG RVPLAPDGTF TATLWAEKGR ANTFEIELTN ATGDRRPVTP GTLTYTVGIV
     ETQPPLTHSI GIGLADNEVE WLFRKGTPLP ARRRTKLSTT VTVSRGSGDG MIRIPVVEGE
     HHRADRNRRI GRLEVDAEQV TRDVPEGSDV EMTIAIDESR LVVARAYVPI LDEEFEHVLN
     LQTESVPAAD DLARDAAAEK RRLAAVRRRV DEFGDARAAA VLARIDAERI VPDLDAEVDA
     ARVDPDAAAA AARRLLDLRA AVDEAEDELE WPQLVQEARE AVPVLREIVR ERGRPGDQPM
     LEAAEDAVQE AITAHDADLL RQRIDELRLL AMRVLDESGD LAFLAFNELE TLQPEMRDRE
     EAGRLVAAGR RAAESGDVDT LRQVNAALGE MLPSPPPPPD PFSTVRRGR
//