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Q89Z59

- T1M_BACTN

UniProt

Q89Z59 - T1M_BACTN

Protein

Probable type I restriction enzyme BthVORF4518P M protein

Gene

BT_4518

Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Methylation of specific adenine residues; required for both restriction and modification activities.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei214 – 2141S-adenosyl-L-methionine1 Publication

    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

    Enzyme and pathway databases

    BioCyciBTHE226186:GJXV-4599-MONOMER.

    Protein family/group databases

    REBASEi7071. M.BthVORF4518P.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable type I restriction enzyme BthVORF4518P M protein (EC:2.1.1.72)
    Short name:
    M.BthVORF4518P
    Gene namesi
    Ordered Locus Names:BT_4518
    OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
    Taxonomic identifieri226186 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
    ProteomesiUP000001414: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 472472Probable type I restriction enzyme BthVORF4518P M proteinPRO_0000310988Add
    BLAST

    Interactioni

    Subunit structurei

    The type I restriction/modification system is composed of three polypeptides R, M and S.By similarity

    Protein-protein interaction databases

    STRINGi226186.BT_4518.

    Structurei

    Secondary structure

    1
    472
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 2414
    Helixi29 – 5123
    Helixi64 – 685
    Helixi73 – 8715
    Helixi91 – 966
    Turni97 – 993
    Helixi107 – 11812
    Helixi128 – 14215
    Turni145 – 1473
    Helixi150 – 1523
    Helixi156 – 16611
    Beta strandi174 – 1763
    Helixi183 – 19311
    Helixi200 – 2078
    Beta strandi210 – 2156
    Helixi217 – 22913
    Beta strandi238 – 2414
    Turni244 – 2463
    Beta strandi253 – 2586
    Beta strandi277 – 2793
    Helixi284 – 29512
    Beta strandi296 – 30712
    Helixi308 – 3125
    Helixi316 – 32712
    Beta strandi328 – 3358
    Beta strandi338 – 3436
    Beta strandi348 – 35710
    Beta strandi360 – 3667
    Beta strandi375 – 3784
    Helixi382 – 3854
    Helixi386 – 3938
    Turni401 – 4033
    Beta strandi408 – 4136
    Helixi414 – 4196
    Helixi421 – 4233

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OKCX-ray2.20A/B1-444[»]
    ProteinModelPortaliQ89Z59.
    SMRiQ89Z59. Positions 7-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ89Z59.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni151 – 1566S-adenosyl-L-methionine binding
    Regioni181 – 1833S-adenosyl-L-methionine binding
    Regioni243 – 2442S-adenosyl-L-methionine binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0286.
    HOGENOMiHOG000295041.
    KOiK03427.
    OMAiCAGHVED.
    OrthoDBiEOG686NCV.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR022749. D12N6_MeTrfase_N.
    IPR003356. DNA_methylase_A-5.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR002296. N12N6_MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF12161. HsdM_N. 1 hit.
    PF02384. N6_Mtase. 1 hit.
    [Graphical view]
    PRINTSiPR00507. N12N6MTFRASE.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS00092. N6_MTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q89Z59-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATNSSTEQS LTKKVWNLAT TLAGQGIGFT DYITQLTYLL FLKMDAENVE    50
    MFGEESAIPT GYQWADLIAF DGLDLVKQYE ETLKLLSELD NLIGTIYTKA 100
    QNKIDKPVYL KKVITMIDEE QWLIMDGDVK GAIYESILEK NGQDKKSGAG 150
    QYFTPRPLIQ AMVDCINPQM GETVCDPACG TGGFLLTAYD YMKGQSASKE 200
    KRDFLRDKAL HGVDNTPLVV TLASMNLYLH GIGTDRSPIV CEDSLEKEPS 250
    TLVDVILANP PFGTRPAGSV DINRPDFYVE TKNNQLNFLQ HMMLMLKTGG 300
    RAAVVLPDNV LFEAGAGETI RKRLLQDFNL HTILRLPTGI FYAQGVKANV 350
    LFFSKGQPTK EIWFYDYRTD IKHTLATNKL ERHHLDDFVS CYNNRVEIYD 400
    AENNPQGRWR KYPVDEIIAR DKTSLDITWI KPGGEVDDRS LAELMADIKD 450
    KSQTISRAVT ELEKLLANIE EN 472
    Length:472
    Mass (Da):53,127
    Last modified:June 1, 2003 - v1
    Checksum:i3891797D2845329D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015928 Genomic DNA. Translation: AAO79623.1.
    RefSeqiNP_813429.1. NC_004663.1.
    WP_011109305.1. NC_004663.1.

    Genome annotation databases

    EnsemblBacteriaiAAO79623; AAO79623; BT_4518.
    GeneIDi1073274.
    KEGGibth:BT_4518.
    PATRICi21064114. VBIBacThe70966_4602.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015928 Genomic DNA. Translation: AAO79623.1 .
    RefSeqi NP_813429.1. NC_004663.1.
    WP_011109305.1. NC_004663.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OKC X-ray 2.20 A/B 1-444 [» ]
    ProteinModelPortali Q89Z59.
    SMRi Q89Z59. Positions 7-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 226186.BT_4518.

    Protein family/group databases

    REBASEi 7071. M.BthVORF4518P.

    Protocols and materials databases

    DNASUi 1073274.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO79623 ; AAO79623 ; BT_4518 .
    GeneIDi 1073274.
    KEGGi bth:BT_4518.
    PATRICi 21064114. VBIBacThe70966_4602.

    Phylogenomic databases

    eggNOGi COG0286.
    HOGENOMi HOG000295041.
    KOi K03427.
    OMAi CAGHVED.
    OrthoDBi EOG686NCV.

    Enzyme and pathway databases

    BioCyci BTHE226186:GJXV-4599-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q89Z59.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR022749. D12N6_MeTrfase_N.
    IPR003356. DNA_methylase_A-5.
    IPR002052. DNA_methylase_N6_adenine_CS.
    IPR002296. N12N6_MeTrfase.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF12161. HsdM_N. 1 hit.
    PF02384. N6_Mtase. 1 hit.
    [Graphical view ]
    PRINTSi PR00507. N12N6MTFRASE.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS00092. N6_MTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
      Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
      Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
    2. "Crystal structure of type I restriction enzyme protein (NP_813429.1) from bacteriodes thetaiotaomicron VPI-5482 at 2.20 A resolution resolution."
      Joint center for structural genomics (JCSG)
      Submitted (JAN-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

    Entry informationi

    Entry nameiT1M_BACTN
    AccessioniPrimary (citable) accession number: Q89Z59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 82 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg2+ as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3