ID M7C298_CHEMY Unreviewed; 443 AA.
AC M7C298;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Histone deacetylase 11 {ECO:0000313|EMBL:EMP38518.1};
GN ORFNames=UY3_04303 {ECO:0000313|EMBL:EMP38518.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP38518.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB519582; EMP38518.1; -; Genomic_DNA.
DR AlphaFoldDB; M7C298; -.
DR STRING; 8469.M7C298; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:InterPro.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR CDD; cd09993; HDAC_classIV; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 2.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR044150; HDAC_classIV.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF33; HISTONE DEACETYLASE 11; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR SUPFAM; SSF52768; Arginase/deacetylase; 2.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 180..396
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
SQ SEQUENCE 443 AA; 49883 MW; 2757A94C0A5A452E CRC64;
MSVYAHLGKL IPLKETIKGF QEILADAYDH LPEQAFYMVG PIKEAVTKAD KLAEEHSPHR
TELYHEVPPT CWPIVYSPDY NITFMGLEKL HPFDAGKWGK VINFLKEEKL IADDLIVQAR
EATEEDLLVV HTRRYLNKLK WSFVVATITE IPPVLFLPNF LVQRKVLKPL RTQTGGTIMG
NGHERDFMDD HRVYIMDVYN RYIYPGDGFA KLKATADNRF APFFLGYLCR CHSMASMEPA
QLTAAVVSIV NTSHIILQYV QNLVMRCQHE DDCEEDVDTD IPESMGCGNW DVMAALGAIK
RKVELDWGTE DTEYLQKVQT HVEGALNELR PDIIIYNAGT DILDGDPLGG LAISPQGIVK
RDEAVFRAAR SHRIPILMVT SGGYQKRTAR IIADSILNLH NLGLIDKELA TSEAKNPKGW
RRLPPEPANG LGELHEVLVS IGN
//