ID M9RA43_9RHOB Unreviewed; 301 AA.
AC M9RA43;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative deacetylase {ECO:0000313|EMBL:AGI67246.1};
GN ORFNames=OAN307_c15730 {ECO:0000313|EMBL:AGI67246.1};
OS Octadecabacter antarcticus 307.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI67246.1, ECO:0000313|Proteomes:UP000005307};
RN [1] {ECO:0000313|EMBL:AGI67246.1, ECO:0000313|Proteomes:UP000005307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=307 {ECO:0000313|EMBL:AGI67246.1,
RC ECO:0000313|Proteomes:UP000005307};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
CC -!- SIMILARITY: Belongs to the histone deacetylase family.
CC {ECO:0000256|ARBA:ARBA00005947}.
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DR EMBL; CP003740; AGI67246.1; -; Genomic_DNA.
DR AlphaFoldDB; M9RA43; -.
DR STRING; 391626.OAN307_c15730; -.
DR KEGG; oat:OAN307_c15730; -.
DR eggNOG; COG0123; Bacteria.
DR HOGENOM; CLU_007727_1_0_5; -.
DR OrthoDB; 9808367at2; -.
DR Proteomes; UP000005307; Chromosome.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:InterPro.
DR CDD; cd09993; HDAC_classIV; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR044150; HDAC_classIV.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF8; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
FT DOMAIN 20..283
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
SQ SEQUENCE 301 AA; 33698 MW; E2226EB2A877DC82 CRC64;
MSQIPVVYND FYDICVPLTH RFNGTKFSKL VHYLQRSDFS NQLDFIHSSP VRYEDIKRAH
ANDYVQRVAT GALLRNEVRQ INLPINTQLI KRSFLALNGT YTTALKALET GVACHAAGGT
HHAHYSHGSG FCVFNDLAFT ALNLIEHGMV ESVLILDLDV HQGDGTIDIC HGKRGIYTCS
LHCEQNFPFQ KRQGTRDVPL DCHLEDNAYL DQLHRTLADI SRDFTPQLVL YDAGVDVFLG
DQLGNLDLTL EGVFKRDCIV LEHFKNCNIP IATVIGGGYS PSDADIARRH LSIFHAAVDV
F
//
