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Database: UniProt
Entry: L0A067_DEIPD
LinkDB: L0A067_DEIPD
Original site: L0A067_DEIPD 
ID   L0A067_DEIPD            Unreviewed;       515 AA.
AC   L0A067;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=E3 binding domain protein {ECO:0000313|EMBL:AFZ66410.1};
GN   OrderedLocusNames=Deipe_0836 {ECO:0000313|EMBL:AFZ66410.1};
OS   Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS   KR-200).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ66410.1, ECO:0000313|Proteomes:UP000010467};
RN   [1] {ECO:0000313|Proteomes:UP000010467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC   {ECO:0000313|Proteomes:UP000010467};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT   19664.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317}.
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DR   EMBL; CP003382; AFZ66410.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0A067; -.
DR   STRING; 937777.Deipe_0836; -.
DR   KEGG; dpd:Deipe_0836; -.
DR   PATRIC; fig|937777.3.peg.843; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_538316_0_0_0; -.
DR   Proteomes; UP000010467; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000010467}.
FT   DOMAIN          12..44
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|Pfam:PF02817"
FT   REGION          55..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..187
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  54183 MW;  2D33C83D1513E22A CRC64;
     MGTKGEGMEM IAPLAKVLAE ANGIDWRHIN GTGQSGLVVE EDILAYLARI MTGEEEPPAT
     PVDAPPPDWN GEMPSMHTLA AAGVDSDIAD FVASARVENA DPTVADLGIA DLASADFGAD
     AMDFELELDE DDQFDSPVTR DPEDMANTPR DADYAGAETL ETPGGTDLPI TPGPLNPGMP
     ARPLTEPATQ PTPGYVDPAQ DAPAHQPSDS DFGLPQDAPT PEETPQDEAQ DEGRSGWHDQ
     QPEEQRTEAA PQTTSSMTGG LLSSLYSKPA QAEPAQSEPA QASQPDFADT PEFEEPEQPP
     VAATHLEPTV VQEAVSTPDV QPEPMQPQVV EPTVVTPPVQ PQATAPTSAV YAEELAAPTA
     QRYATLRLSF DASALSSART HLAEHFERPA PLSVFVARAA SRRIDLLKLQ SVGVYGVGDE
     VLPVATPNLT ADFRAAVDDL HGAEGGQLSD LMVVDAGELG LDELQLPAGD LTLSLGRIRD
     GSATLTLTGP VSVRSGASFL QGVAELLETP IRLML
//
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