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P14751

- MTR1_RHOSH

UniProt

P14751 - MTR1_RHOSH

Protein

Modification methylase RsrI

Gene

rsrIM

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    This methylase recognizes the double-stranded sequence GAATTC, causes specific methylation on A-? on both strands, and protects the DNA from cleavage by the RsrI endonuclease.

    Catalytic activityi

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

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. N-methyltransferase activity Source: InterPro
    3. 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

    REBASEi3487. M.RsrI.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Modification methylase RsrI (EC:2.1.1.72)
    Short name:
    M.RsrI
    Alternative name(s):
    Adenine-specific methyltransferase RsrI
    Gene namesi
    Name:rsrIM
    OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
    Taxonomic identifieri1063 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 319319Modification methylase RsrIPRO_0000087970Add
    BLAST

    Structurei

    Secondary structure

    1
    319
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 447
    Helixi47 – 526
    Beta strandi59 – 646
    Helixi72 – 765
    Helixi81 – 9515
    Beta strandi96 – 10611
    Helixi119 – 12911
    Beta strandi133 – 1419
    Beta strandi149 – 1513
    Beta strandi156 – 16510
    Helixi173 – 1753
    Helixi181 – 1888
    Helixi195 – 2006
    Beta strandi206 – 2094
    Helixi229 – 23911
    Beta strandi245 – 2484
    Turni252 – 2543
    Helixi255 – 2639
    Beta strandi266 – 2738
    Helixi275 – 28612
    Beta strandi299 – 3035
    Helixi305 – 3084
    Helixi309 – 3124

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EG2X-ray1.75A1-319[»]
    1NW5X-ray2.05A1-319[»]
    1NW6X-ray1.94A1-319[»]
    1NW7X-ray2.10A1-319[»]
    1NW8X-ray2.25A1-319[»]
    ProteinModelPortaliP14751.
    SMRiP14751. Positions 36-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14751.

    Family & Domainsi

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR002295. D21N6_MeTrfase.
    IPR002941. DNA_methylase_N4/N6.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF01555. N6_N4_Mtase. 1 hit.
    [Graphical view]
    PRINTSiPR00506. D21N6MTFRASE.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14751-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANRSHHNAG HRAMNALRKS GQKHSSESQL GSSEIGTTRH VYDVCDCLDT    50
    LAKLPDDSVQ LIICDPPYNI MLADWDDHMD YIGWAKRWLA EAERVLSPTG 100
    SIAIFGGLQY QGEAGSGDLI SIISHMRQNS KMLLANLIIW NYPNGMSAQR 150
    FFANRHEEIA WFAKTKKYFF DLDAVREPYD EETKAAYMKD KRLNPESVEK 200
    GRNPTNVWRM SRLNGNSLER VGHPTQKPAA VIERLVRALS HPGSTVLDFF 250
    AGSGVTARVA IQEGRNSICT DAAPVFKEYY QKQLTFLQDD GLIDKARSYE 300
    IVEGAANFGA ALQRGDVAS 319
    Length:319
    Mass (Da):35,655
    Last modified:April 1, 1990 - v1
    Checksum:i806E7BF702D4EC85
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16456 Genomic DNA. Translation: CAA34475.1.
    PIRiS07570.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16456 Genomic DNA. Translation: CAA34475.1 .
    PIRi S07570.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EG2 X-ray 1.75 A 1-319 [» ]
    1NW5 X-ray 2.05 A 1-319 [» ]
    1NW6 X-ray 1.94 A 1-319 [» ]
    1NW7 X-ray 2.10 A 1-319 [» ]
    1NW8 X-ray 2.25 A 1-319 [» ]
    ProteinModelPortali P14751.
    SMRi P14751. Positions 36-314.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    REBASEi 3487. M.RsrI.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P14751.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR002295. D21N6_MeTrfase.
    IPR002941. DNA_methylase_N4/N6.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF01555. N6_N4_Mtase. 1 hit.
    [Graphical view ]
    PRINTSi PR00506. D21N6MTFRASE.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification, cloning and sequence analysis of RsrI DNA methyltransferase: lack of homology between two enzymes, RsrI and EcoRI, that methylate the same nucleotide in identical recognition sequences."
      Kaszubska W., Aiken C., O'Connor D., Gumport R.I., Stephenson F.H., Greene P.J.
      Nucleic Acids Res. 17:10403-10425(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 630.
    2. "Nucleotide sequence of the gene encoding the RsrI methyltransferase."
      Stephenson F.H., Greene P.J.
      Nucleic Acids Res. 17:10503-10503(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 630.
    3. "Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases."
      Scavetta R.D., Thomas C.B., Walsh M.A., Szegedi S., Joachimiak A., Gumport R.I., Churchill M.E.
      Nucleic Acids Res. 28:3950-3961(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

    Entry informationi

    Entry nameiMTR1_RHOSH
    AccessioniPrimary (citable) accession number: P14751
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Restriction enzymes and methylases
      Classification of restriction enzymes and methylases and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3