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Q55AX2

- DOT1L_DICDI

UniProt

Q55AX2 - DOT1L_DICDI

Protein

Histone-lysine N-methyltransferase, H3 lysine-79 specific

Gene

dotA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing, correct growth and development, and for resistance to DNA damage induced by UV LIGHT.1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].By similarityPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1300 – 13001S-adenosyl-L-methionineBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. histone methyltransferase activity (H3-K79 specific) Source: dictyBase

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: dictyBase
    2. DNA repair Source: UniProtKB-KW
    3. histone H3-K79 methylation Source: dictyBase
    4. regulation of sorocarp development Source: dictyBase
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase, H3 lysine-79 specific1 Publication (EC:2.1.1.43By similarity)
    Alternative name(s):
    Disruptor of telomeric silencing A1 Publication
    Histone H3-K79 methyltransferaseBy similarity
    Short name:
    H3-K79-HMTaseBy similarity
    SAM domain-containing proteinImported
    Gene namesi
    Name:dotAImported
    Synonyms:dot11 Publication, KMT41 Publication
    ORF Names:DDB_G0271626
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 2, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0271626. dotA.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: dictyBase

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Individuals exhibit 4-5 hours delay in development. Development does progress with fewer fruiting bodies and smaller spore heads. No apparent changes in cell cycle regulation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18451845Histone-lysine N-methyltransferase, H3 lysine-79 specificPRO_0000413849Add
    BLAST

    Expressioni

    Developmental stagei

    Expressed during the whole life cycle.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDBDRAFT_0216874.

    Structurei

    3D structure databases

    ProteinModelPortaliQ55AX2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1125 – 1446322DOT1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni625 – 63915Required for interaction with nucleosomes and DNABy similarityAdd
    BLAST
    Regioni1251 – 12544S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
    Regioni1274 – 128310S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi37 – 7337Asn-richSequence AnalysisAdd
    BLAST
    Compositional biasi90 – 226137Ser-richSequence AnalysisAdd
    BLAST
    Compositional biasi121 – 16040Gln-richSequence AnalysisAdd
    BLAST
    Compositional biasi195 – 26369Asn-richSequence AnalysisAdd
    BLAST
    Compositional biasi336 – 449114Thr-richSequence AnalysisAdd
    BLAST
    Compositional biasi454 – 46916Asn-richSequence AnalysisAdd
    BLAST
    Compositional biasi464 – 676213Arg/Glu/Lys-richAdd
    BLAST
    Compositional biasi730 – 77142Asn-richSequence AnalysisAdd
    BLAST
    Compositional biasi832 – 86231Gln-richSequence AnalysisAdd
    BLAST
    Compositional biasi863 – 88018Thr-richSequence AnalysisAdd
    BLAST
    Compositional biasi965 – 1065101Asn-richSequence AnalysisAdd
    BLAST
    Compositional biasi1467 – 1659193Ser-richSequence AnalysisAdd
    BLAST
    Compositional biasi1489 – 150113Thr-richSequence AnalysisAdd
    BLAST
    Compositional biasi1521 – 155636Asn-richSequence AnalysisAdd
    BLAST
    Compositional biasi1772 – 184473Asn-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. DOT1 family.PROSITE-ProRule annotation
    Contains 1 DOT1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiKOG3924.
    InParanoidiQ55AX2.
    OMAiLEISIME.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR013110. DOT1.
    IPR025789. Histone_H3-K79_MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF08123. DOT1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51569. DOT1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q55AX2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTNSTPRKQ KLSNSKSLQN SPISPTVKKT NSFPLGNNIP TNINRSKKDK     50
    NNNSNNNINN NNSNGIGSNT IINSTPIATT PVPPLPFIHS SSSSSSSPSP 100
    SSSSSSPFPK AKKSPSLSIN QQQQQQPQQP QQSPQSQQSP QSQQSQQSQQ 150
    QQPQQPQEQQ EPLPNLSFLR NQEPDKNVLP TSRKRPPSVM PSTPNQSSNS 200
    SSLNSSLNFS SSNSSPSPTS TQSNNSRFET RSQNDQYENN NNNNNNNNNN 250
    NNNNNNNNNN NNNIECIVID DDDDDDDDEG NSIKSTHTST QSTPIRDRRQ 300
    RDNKWTINPL PQFQREIIDV DTPSPPNESL SIVSQTTTNT ITDTTSIQTP 350
    TLIRQSSSLL SSSSSLSPST TSTPLTQNNI NLQNAQVIAT MTAPMEIELP 400
    TIVQLEPLFS SEFTTSTQNL FIQTPPFTST LTLPTTTAQT SQTLFTIQTS 450
    HDINNNNNNN NNNKNKNKNK KEIEKEKEKL REALKQKLKE YENENEKERE 500
    KERKREREIE IERERKERER KEREKERKKE KEREREREER ERKEIERKER 550
    EREEREERER KEIERKETER KEIERKEIER KEIERKERER KERKEREERE 600
    EREREERERK EREEREKEIE MEREKKKEKE KEKEKEKEKE KEKEKEKEKE 650
    KEKEKEKEKK RKENEVENEI EKERREKNDS YMVLNYHHSI DDHHSESESE 700
    SDSDQDSIYS ISTQELSSVI SDNDFCDSDN EKVANNNRTV GETFLNDSRN 750
    NNNNNNNNKN NNNKKIENDK NQLIERERLI SAFNDKAFLY ALDTIREVLG 800
    GIDFKLKVSK EQIIEISTNA KKPLNILSEP EQQQQQQQQQ QQQQHQQQQQ 850
    QQQQQQQQQQ QQTTKTTTTT NNTTTTTAET EKPKEVFLLK KPIKIPYGRD 900
    CKKRLIRRFH GTSRNPLFHK NLESTLKLLK RAKFDWASIE FDTKSYLMNC 950
    NCKTVCHKSE RMKDNPTNKL QNNNRNNNNN NNNIINNNNN NNNKNNNNKN 1000
    NNNKNNNRNN NSIAKKIGTN NNNNNTTIIK NNNNNNNNNN NNNNNNNNII 1050
    KNNNNNNKNN NNNNNTIVKK IETIKKDINK KPTKTTTTTS SSSSSTSSSN 1100
    SLTVIKKPVK KINGSQRICL FEDDFDVGIG VPVTTGTSET TTTRASSIRR 1150
    KMNISNIFDD FTKKPRQNKY NEIEMPDLFA SKECNYTLEQ QAPFIRAQKL 1200
    LLTQQHENNL YNGKRFMKYD EWLDLYHGEM RSSIQNPKVL KHYISFSQEV 1250
    YGEAEPTLLR HWIHLGLIKP TDVFCDIGCG IGNVLFQLAA QVGCRVIGVE 1300
    IRKDLYDISQ SMLEIYKKRS LELGLHPSTQ QIKIYNCDVK GSLEFDFSEP 1350
    NVFFMHNTCF GPELEISIME LFKKYSKPGT KVITMKTLCP RFKPSDKKTK 1400
    PWGIFKYPYE SYEMEEGSLS WRSATNCSFY SFTIDDKDSD IVTDQTHLNR 1450
    VILSTPKKKH SKLQLFSSSS LPSSPPSSSS SSSPPNIATN TTTTTTTTTT 1500
    TSPSSISLPS PYLSPSKKTP NSNKRDRSDI DNSNSDDGDE NNNNININNN 1550
    NNNSNNKPIK LKLSMDHSID NQSNSESSDT DVEYMPWSKR NNRKKRKSLS 1600
    YSLDSYLSSR ISPSLSLSTS SSSSSSLDSS PYSSPPSSSS SDNENDDDNG 1650
    DDEDDSSSSN DTKLKEKLLL MKNNEKIGGA PPLTRRNANS DTNKLVQGCY 1700
    QSLSSYALPK EESQIHKLQL QAKLLEHKNS LVLKHQKSIH DQQKRLSRKQ 1750
    KKLAKKNKKK EQQLQAQAKT INYNNNNNNN NQNDNQVNHN NLNENEINTD 1800
    LINGYNNNNN NNIINNDNDN DNDNDKDDDK DSNNKDYNNI NDNNK 1845
    Length:1,845
    Mass (Da):212,281
    Last modified:May 2, 2006 - v2
    Checksum:i6CDF92C0D67AAD87
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000006 Genomic DNA. Translation: EAL71677.2.
    RefSeqiXP_645574.2. XM_640482.2.

    Genome annotation databases

    EnsemblProtistsiDDB0233511; DDB0233511; DDB_G0271626.
    GeneIDi8618027.
    KEGGiddi:DDB_G0271626.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000006 Genomic DNA. Translation: EAL71677.2 .
    RefSeqi XP_645574.2. XM_640482.2.

    3D structure databases

    ProteinModelPortali Q55AX2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDBDRAFT_0216874.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0233511 ; DDB0233511 ; DDB_G0271626 .
    GeneIDi 8618027.
    KEGGi ddi:DDB_G0271626.

    Organism-specific databases

    dictyBasei DDB_G0271626. dotA.

    Phylogenomic databases

    eggNOGi KOG3924.
    InParanoidi Q55AX2.
    OMAi LEISIME.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR013110. DOT1.
    IPR025789. Histone_H3-K79_MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF08123. DOT1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS51569. DOT1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    2. "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.
    3. "The histone methyltransferase Dot1 is required for DNA damage repair and proper development in Dictyostelium."
      Muller-Taubenberger A., Bonisch C., Furbringer M., Wittek F., Hake S.B.
      Biochem. Biophys. Res. Commun. 404:1016-1022(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
      Strain: AX21 Publication.

    Entry informationi

    Entry nameiDOT1L_DICDI
    AccessioniPrimary (citable) accession number: Q55AX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2011
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 57 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    In contrast to other lysine histone methyltransferases, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.1 Publication

    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