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)

A9VA99

- A9VA99_MONBE

UniProt

A9VA99 - A9VA99_MONBE

Protein

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

Gene

34214

Organism
Monosiga brevicollis (Choanoflagellate)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 28 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. histone-lysine N-methyltransferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Chromatin regulatorUniRule annotation, MethyltransferaseUniRule annotation, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionineUniRule annotation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase, H3 lysine-79 specificUniRule annotation (EC:2.1.1.43UniRule annotation)
    Alternative name(s):
    Histone H3-K79 methyltransferaseUniRule annotation
    Gene namesi
    ORF Names:34214Imported
    OrganismiMonosiga brevicollis (Choanoflagellate)Imported
    Taxonomic identifieri81824 [NCBI]
    Taxonomic lineageiEukaryotaChoanoflagellidaCodonosigidaeMonosiga
    ProteomesiUP000001357: Unassembled WGS sequence

    Subcellular locationi

    Nucleus UniRule annotation

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    NucleusUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi81824.JGI34214.

    Structurei

    3D structure databases

    ProteinModelPortaliA9VA99.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG294902.
    KOiK11427.

    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.

    A9VA99-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASAEAEVS QSKPSPLKDQ AGPVQPRPAG LTPGNPVQAV VEEAASPCAS    50
    SPQAPSSAPN SHRRPVGGRI GRVHLGQPGR RVPDEEDVEA IPGGSRELGI 100
    TEDWFDVPPL FPPVDTTQTH LAILSPNPKG PPMLYQWPFT HMTDSSYDAG 150
    FELLNSMNHI VKLCALPVPD TWADDIVACA KPGTEFASLS KVVEAFNAAM 200
    RVYHKSVGEQ AERLICPTDL CEHIMNMTYS RAVTDPALLN RYKGWTAEVY 250
    GEFTSKMISD VIANSNVQPD DTFVDLGSGV GQVVLQVALE GRARTSFGIE 300
    KQDIPAEYAK CGAYELVKDN FLQPQYAERI TNTSVVFLNN FAFGTKVNQQ 350
    LCRMFENCQA GTRLISSISL RKSDFTITAR TLNDLGCILT MRKLCYRGQG 400
    VSWTARPFSY YVQTVNHQYL DQFFSKGEPV QVPFENEVGD DDDDANPDRT 450
    GTSHSGAPVR DNSDDEEDND EEAEDQSAGA AGHHKTDAVG KGHSGAERDG 500
    KAAAGTRPGS TKRSKGASRR RDRQSSQQSS APPSSSSGKV AAGDDSASQR 550
    LVRTLTRAVA GLERRYPSGR TLRAARHQLR ALHQERSVLR QHRREYEQQL 600
    QQHNQTVAAA LTQRRQQLNE SLGLDSKTDT RLTAAAAGLL HTFVCRGGQS 650
    ATSSAANAQQ SVEHIRLWTK PLQQAQAVHE RLIAALRMHG QAPVADALQR 700
    TPWALPRDLC ASNEHSPTRA TNGHVPVQEA SAGKAGPTGP HQSARRSSDQ 750
    NGSASSQVQS AQTRGLEATP DRYAGPLSSA ETSPASTSSH SAGKRDLSGQ 800
    REATNGTEHT SQAQIAGRRE SSSTGTSPTS SLAKLLGAEP SHRSGHRQGQ 850
    QRPIARAREM RPPGGARPGL SSSSKRPLSS NGEPAPQVPD PKRTKDLENA 900
    SSDNALERKQ KCHGPETSN 919
    Length:919
    Mass (Da):99,082
    Last modified:February 5, 2008 - v1
    Checksum:i529CA3D95C972687
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH991573 Genomic DNA. Translation: EDQ85503.1.
    RefSeqiXP_001749694.1. XM_001749642.1.

    Genome annotation databases

    GeneIDi5894943.
    KEGGimbr:MONBRDRAFT_34214.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH991573 Genomic DNA. Translation: EDQ85503.1 .
    RefSeqi XP_001749694.1. XM_001749642.1.

    3D structure databases

    ProteinModelPortali A9VA99.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 81824.JGI34214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5894943.
    KEGGi mbr:MONBRDRAFT_34214.

    Phylogenomic databases

    eggNOGi NOG294902.
    KOi K11427.

    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: MX1 / ATCC 50154Imported.

    Entry informationi

    Entry nameiA9VA99_MONBE
    AccessioniPrimary (citable) accession number: A9VA99
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 5, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 28 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    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.UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3