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P58284

- MTA1_AZOBR

UniProt

P58284 - MTA1_AZOBR

Protein

Modification methylase AbrI

Gene

abrIM

Organism
Azospirillum brasilense
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
  1. Functioni

    This methylase recognizes the double-stranded sequence CTCGAG, causes specific methylation on A-5 on both strands, and protects the DNA from cleavage by the AbrI endonuclease.Curated

    Catalytic activityi

    S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

    GO - Molecular functioni

    1. site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC

    GO - Biological processi

    1. DNA restriction-modification system Source: UniProtKB-KW

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Restriction system

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Protein family/group databases

    REBASEi4924. M.AbrI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase AbrI (EC:2.1.1.72)
    Short name:
    M.AbrI
    Alternative name(s):
    Adenine-specific methyltransferase AbrI
    Gene namesi
    Name:abrIM
    OrganismiAzospirillum brasilense
    Taxonomic identifieri192 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 140›140Modification methylase AbrIPRO_0000087942Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP58284.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the N(4)/N(6)-methyltransferase family.Curated

    Sequencei

    Sequence statusi: Fragment.

    P58284-1 [UniParc]FASTAAdd to Basket

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    YRTIDRIYPA LTREHKLLIP DIKGEAHIVY EEGRLYPHHN LYYITSEIWD    50
    LRALQAVLLS GIARLFVSVY STKMHGGFLR FQAQYLRRIR VPNWSQVPAA 100
    VRQELITAGA KPDLAACNRA VFALYAMTAE ERAALGGNGD 140
    Length:140
    Mass (Da):15,900
    Last modified:September 26, 2001 - v1
    Checksum:i7B5BC7D96697E174
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62690 Genomic DNA. No translation available.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62690 Genomic DNA. No translation available.

    3D structure databases

    ProteinModelPortali P58284.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 4924. M.AbrI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "AbrI restriction modification system from Azospirillium brasilense, molecular cloning and characterization of its genes."
      Schwabe G., Helke A., Klingmueller W.
      Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 29711 / DSM 1844.

    Entry informationi

    Entry nameiMTA1_AZOBR
    AccessioniPrimary (citable) accession number: P58284
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 32 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Restriction enzymes and methylases
      Classification of restriction enzymes and methylases and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3