GenomeNet

Database: UniProt/TrEMBL
Entry: E3JXV3_PUCGT
LinkDB: E3JXV3_PUCGT
Original site: E3JXV3_PUCGT 
ID   E3JXV3_PUCGT            Unreviewed;       632 AA.
AC   E3JXV3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN   ORFNames=PGTG_02339 {ECO:0000313|EMBL:EFP76878.2};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP76878.2, ECO:0000313|Proteomes:UP000008783};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRL 75-36-700-3;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA   Schein J.;
RT   "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT   700-3.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000256|ARBA:ARBA00006457}.
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; DS178266; EFP76878.2; -; Genomic_DNA.
DR   RefSeq; XP_003321297.2; XM_003321249.2.
DR   AlphaFoldDB; E3JXV3; -.
DR   STRING; 418459.E3JXV3; -.
DR   EnsemblFungi; EFP76878; EFP76878; PGTG_02339.
DR   GeneID; 10529063; -.
DR   KEGG; pgr:PGTG_02339; -.
DR   VEuPathDB; FungiDB:PGTG_02339; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_0_1_1; -.
DR   InParanoid; E3JXV3; -.
DR   OrthoDB; 1327607at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; IBA:GO_Central.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR48252; HISTONE DEACETYLASE 2-RELATED; 1.
DR   PANTHER; PTHR48252:SF57; HISTONE DEACETYLASE HDAC1; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT   DOMAIN          33..321
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          399..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..496
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..536
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   632 AA;  69733 MW;  6975033F4757C690 CRC64;
     MSGNMIPIAG EDKKRICYFF DSDIGNYHYG PGHPMKPHRI RMTHALVMNY GLYKKMEIFR
     AKPATRKEMA QFHTDDYVDF LSKVTPDNME EFAKEQAKFN LGDDCPVFDG LFEYCSISAG
     GSMEGAARLS RDKCDIAVNW AGGLHHAKKA EANGFCYVND IVLGILELLR YHKRVLYVDI
     DVHHGDGVEE AFYTTDRVMT CSFHKYGEFF PGTGELRDTG HGKGKHYAVN FPLRDGITDE
     AYKNIFEPVI MKIMETYQPS AIVLQCGGDS LSGDRLGSFN VSMRGHANCV RFIKSLGLPL
     LLLGGGGYTI RNVSRTWAYE TGLAAGQELC TDIPMNEYYE YFGPTYRLDV PPSNMEDMNV
     VKYLEKTKIQ IFENLRHTIP VPSVGLQAIP RLAHDEMDVD EDLDDPNERR PQRLLDGLIQ
     RDDEFSDSED EGEGGRRDIQ SHKRARRQSP KMNGNGILSI HSGIQNSFSQ SRHSADLHFN
     RPSSSHNSSL SVDTPDPPIV TPTPDPTIAA PTPDPPVTAP APDPPITQPA PDLVVGPEPG
     PSALRPTLDP PTVGPIANPH VVPLVPDPRV VTPVAAQPVV VPVEVPPVVV PVAATPIVAP
     TPTTALVDIP MLSQVDQMEL EKLTSEAFNA QI
//
DBGET integrated database retrieval system