Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q54VQ7

- HDA22_DICDI

UniProt

Q54VQ7 - HDA22_DICDI

Protein

Type-2 histone deacetylase 2

Gene

hdaC

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes By similarity.By similarity

    Catalytic activityi

    Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1165 – 11651SubstrateBy similarity
    Binding sitei1227 – 12271Substrate; via carbonyl oxygenBy similarity
    Metal bindingi1256 – 12561Divalent metal cationBy similarity
    Metal bindingi1258 – 12581Divalent metal cationBy similarity
    Metal bindingi1350 – 13501Divalent metal cationBy similarity

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. metal ion binding Source: UniProtKB-KW
    3. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    4. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    5. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    6. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Type-2 histone deacetylase 2 (EC:3.5.1.98)
    Short name:
    DdHdaC
    Gene namesi
    Name:hdaC
    ORF Names:DDB_G0280195
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 3, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0280195. hdaC.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17041704Type-2 histone deacetylase 2PRO_0000331372Add
    BLAST

    Proteomic databases

    PRIDEiQ54VQ7.

    Expressioni

    Developmental stagei

    Expressed after cells enter the multicellular phase upon starvation.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDBDRAFT_0206434.

    Structurei

    3D structure databases

    ProteinModelPortaliQ54VQ7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi25 – 306Poly-Asn
    Compositional biasi45 – 5511Poly-AsnAdd
    BLAST
    Compositional biasi58 – 6811Poly-AsnAdd
    BLAST
    Compositional biasi225 – 23713Poly-AsnAdd
    BLAST
    Compositional biasi246 – 28641Poly-AsnAdd
    BLAST
    Compositional biasi360 – 3678Poly-Glu
    Compositional biasi543 – 5497Poly-Gln
    Compositional biasi561 – 57919Poly-AsnAdd
    BLAST
    Compositional biasi673 – 6808Poly-Gln
    Compositional biasi1037 – 10404Poly-Thr
    Compositional biasi1489 – 150618Poly-GlnAdd
    BLAST
    Compositional biasi1513 – 153422Thr-richAdd
    BLAST
    Compositional biasi1540 – 15489Poly-Asn
    Compositional biasi1551 – 156818Poly-AsnAdd
    BLAST
    Compositional biasi1585 – 161632Poly-AsnAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0123.
    OMAiNSEFETH.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    3.40.800.20. 1 hit.
    InterProiIPR017956. AT_hook_DNA-bd_motif.
    IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PRINTSiPR01270. HDASUPER.
    SMARTiSM00384. AT_hook. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q54VQ7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTNNIIEGD EDTKTTITNE SNTDNNNNNN DDNKNNTENT TSPTNNNNTN     50
    DNDNNSDNNN NKNNNNNNSQ VTEEQQVTLE DSGSEDDINF EEHELSDSAE 100
    EDEDEMEDDD EDADGRQNQN PNSAGGKRRG RPSKVQQSTN THLSQTTPES 150
    PTIFTPDGKV PKRISTSTNN TPNTQSALKT NKRPRLTSDE EKDLMLSEES 200
    DGGVGEDDDS IMSTNDKPQD ENQSNQNQNN NNNNNNNTTT TTTTTNNSNN 250
    NNQNLNQNNN NNNNNNNINN NNNNNNSNND NNNNNNRPAR GRPKTNGSRS 300
    EERKRIQLQQ YIQATQGSST TTSDPNNQNN QINQINQNNQ NNQNNQNNQN 350
    NSLGEEEFGE EFEEEEEDMG QPKKKTKYKT SKKSVPNHLD IRPCWFVGCV 400
    KADRSLKILR PCLIPTCKTH AIKSEVRISE ALRRGDFVND ESSGVKDKVC 450
    GICGDKKDLH HCGNNGCAFG FCNDCVEIAA MKHNNHPNGN KWICWVCQFV 500
    RTKAKEKERT RWVKEQLNPG LTSISRKFRR GPELDMAQAQ FLQQQQQQQT 550
    SPNEKRSSQF NSNNSNNNNN NNSNNNNNNS GFDPSGSPNN QQNQKRLRKK 600
    INASSDIYET RKYTKKRNDE DSAPPSPTSI IGNSVMVGSS GAAGGGIIKN 650
    TTVVVEQQGY SATPPSPNTL MVQQQQQLQQ THQQARLSQQ QAQLQQLKAL 700
    QQQHQHQQQN NGNFNNLIES VLSPNREPLN PIDNFVDQTF TAVKFFSTLS 750
    QNPPDEIKER IDNFVDLMMR IKTVRWASDY GLVWRMIEEL SNLIKRNLLS 800
    SQSVVEMYSE LKSLEEGALE NMTTNARNVP LERAITMVFE NHETAGLIGK 850
    ECCSTRNALI YSIEVALRAI ADYQHDLEDN LMEESLRSNK VSTEIEQIEH 900
    QIKANLDEIH KFKYQEVELL DSLSKVRGAI AAHESIRDTL QKKSSELKVD 950
    MLLIKNGISD KEKETKSQQA TLENEIYALK LLITMVESIY WIHDYFYESR 1000
    VGECEKLINN KLSQLQNKLE TQIPHPPNAL DNAIPNTTTT VMGEDGQPVI 1050
    VPTTVDIKNK FKTIAIYHKI CMQHKVPNFH LEKPDRIQVA VSCINEFASN 1100
    PLVDIFDNPP EVDMRYVMAV HDANYIKKLE TSLPPENSEF ETHLESDKSG 1150
    AMVTVASHKD FEGDDDNIYD TFVSHRSIKA ALRASGSVCA AVDSVSRSGY 1200
    TRAFCAIRPP GHHAGRYGRT SDAPSQGYCL INNVAIGAKY ASLTAGYSRI 1250
    AVVDFDVHHG NGTQEILSGD DNFLFISIHV CDEKRYFYPG TGQDVGDIDE 1300
    VSGQFDGNIL NIGLKRNTGS AVFLQQWMNK IIPRLEAYKP QLIFLSAGFD 1350
    GHKDDPTNGL KLNEEDYFVI TKMIKTVAFK YCKGRIISVL EGGYGIEKTN 1400
    SLQRCVNSHL KALIEDTDEE IHLANISYGH FSETQETAIP KFNINNFISN 1450
    PNKRGKKNNL NTINFINNNM NNINNNITNS LSNKQLERQK QLQQQQQQAQ 1500
    QAQQQQSPQQ SQTIENTSIT TTTTTTSTTT TLSTSDSESN NNINNNNNDY 1550
    NNNNNNNSNN NNNNSNNNQP TNFNSSTSSP ILSGNNNNNN NNNNNNNNNN 1600
    INNNNNNNSN NNNNMNTSNP TNQQSSVIIS DDMDDVQTNS NPPNPQYPLS 1650
    PNSVNRGNNP SNISMSGAQR SAPLIISPKP SNSPNSPSTS NNNGTPQNIN 1700
    NSDN 1704
    Length:1,704
    Mass (Da):190,816
    Last modified:May 24, 2005 - v1
    Checksum:i84E83B42FB36896E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000035 Genomic DNA. Translation: EAL67324.1.
    RefSeqiXP_641298.1. XM_636206.1.

    Genome annotation databases

    EnsemblProtistsiDDB0237658; DDB0237658; DDB_G0280195.
    GeneIDi8622431.
    KEGGiddi:DDB_G0280195.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000035 Genomic DNA. Translation: EAL67324.1 .
    RefSeqi XP_641298.1. XM_636206.1.

    3D structure databases

    ProteinModelPortali Q54VQ7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDBDRAFT_0206434.

    Proteomic databases

    PRIDEi Q54VQ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0237658 ; DDB0237658 ; DDB_G0280195 .
    GeneIDi 8622431.
    KEGGi ddi:DDB_G0280195.

    Organism-specific databases

    dictyBasei DDB_G0280195. hdaC.

    Phylogenomic databases

    eggNOGi COG0123.
    OMAi NSEFETH.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    3.40.800.20. 1 hit.
    InterProi IPR017956. AT_hook_DNA-bd_motif.
    IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PRINTSi PR01270. HDASUPER.
    SMARTi SM00384. AT_hook. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    2. "Histone deacetylases regulate multicellular development in the social amoeba Dictyostelium discoideum."
      Sawarkar R., Visweswariah S.S., Nellen W., Nanjundiah V.
      J. Mol. Biol. 391:833-848(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiHDA22_DICDI
    AccessioniPrimary (citable) accession number: Q54VQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3