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Protein

mRNA cap guanine-N7 methyltransferase

Gene

ABD1

Organism
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation

Kineticsi

  1. KM=1 mM for GTP1 Publication
  2. KM=25 µM for S-adenosyl-L-methionine1 Publication
  3. KM=0.1 mM for cap dinucleotide GpppA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391S-adenosyl-L-methionine
    Binding sitei57 – 571S-adenosyl-L-methionine; via carbonyl oxygen
    Sitei60 – 601mRNA cap binding
    Sitei66 – 661mRNA cap binding
    Binding sitei79 – 791S-adenosyl-L-methionine
    Sitei91 – 911mRNA cap binding
    Binding sitei129 – 1291mRNA cap
    Binding sitei210 – 2101mRNA cap
    Binding sitei269 – 2691mRNA cap

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    mRNA capping, mRNA processing

    Keywords - Ligandi

    RNA-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.56. 7412.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    mRNA cap guanine-N7 methyltransferase (EC:2.1.1.56)
    Alternative name(s):
    mRNA (guanine-N(7)-)-methyltransferase
    mRNA cap methyltransferase
    Gene namesi
    Name:ABD1
    Ordered Locus Names:ECU10_0380
    OrganismiEncephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite)
    Taxonomic identifieri284813 [NCBI]
    Taxonomic lineageiEukaryotaFungiMicrosporidiaUnikaryonidaeEncephalitozoon
    Proteomesi
    • UP000000819 Componenti: Chromosome X

    Organism-specific databases

    EuPathDBiMicrosporidiaDB:ECU10_0380.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321R → A: No effect. Loss of activity; when associated with A-60. 1 Publication
    Mutagenesisi35 – 351N → A: No effect. Loss of activity; when associated with A-269. 1 Publication
    Mutagenesisi36 – 361N → A: Reduces activity by 85%. 2 Publications
    Mutagenesisi36 – 361N → D: Reduces activity by 96%. 2 Publications
    Mutagenesisi39 – 391K → A, Q or R: Loss of activity. 3 Publications
    Mutagenesisi55 – 551D → A or N: Reduces activity by 95%. 2 Publications
    Mutagenesisi55 – 551D → E: Reduces activity by 60%. 2 Publications
    Mutagenesisi60 – 601K → A: Reduces activity by 92%. Loss of activity; when associated with A-32. 2 Publications
    Mutagenesisi63 – 631D → A or N: Reduces activity by 99%. 3 Publications
    Mutagenesisi63 – 631D → E: Reduces activity by 75%. 3 Publications
    Mutagenesisi66 – 661K → A: Reduces activity by 80%. 2 Publications
    Mutagenesisi66 – 661K → Q or R: Reduces activity by 90%. 2 Publications
    Mutagenesisi79 – 791D → A or N: Loss of activity. 3 Publications
    Mutagenesisi79 – 791D → E: Reduces activity by 77%. 3 Publications
    Mutagenesisi80 – 801I → A: No effect. Strongly reduced activity; when associated with A-109. 1 Publication
    Mutagenesisi91 – 911R → A or Q: Reduces activity by over 98%. 2 Publications
    Mutagenesisi91 – 911R → K: Reduces activity by 96%. 2 Publications
    Mutagenesisi107 – 1082DS → AA: Slightly reduced activity. 1 Publication
    Mutagenesisi109 – 1091Y → A: Reduces activity by 83%. Strongly reduced activity; when associated with A-80. 2 Publications
    Mutagenesisi126 – 1261F → A or N: Loss of activity. 2 Publications
    Mutagenesisi126 – 1261F → H: Reduces activity by 92%. 2 Publications
    Mutagenesisi126 – 1261F → I: Reduces activity by 75%. 2 Publications
    Mutagenesisi126 – 1261F → L: Reduces activity by 55%. 2 Publications
    Mutagenesisi126 – 1261F → V: Reduces activity by 84%. 2 Publications
    Mutagenesisi129 – 1291H → A: Reduces activity by 53%. Reduces activity by 99%; when associated with L-130. 1 Publication
    Mutagenesisi130 – 1301Y → A, S or V: Reduces activity by 98%. 1 Publication
    Mutagenesisi130 – 1301Y → F: Reduces activity by 66%. 1 Publication
    Mutagenesisi130 – 1301Y → L: Reduces activity by 99%; when associated with A-129. 1 Publication
    Mutagenesisi201 – 2011L → A: No effect. 1 Publication
    Mutagenesisi210 – 2101E → A: Reduces activity by 87%. 1 Publication
    Mutagenesisi269 – 2691Y → A: Reduced activity. Loss of activity; when associated with A-35. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 283283mRNA cap guanine-N7 methyltransferasePRO_0000210142Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi284813.NP_586153.1.

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi29 – 4618Combined sources
    Beta strandi52 – 565Combined sources
    Turni59 – 635Combined sources
    Helixi64 – 707Combined sources
    Beta strandi73 – 808Combined sources
    Helixi82 – 9312Combined sources
    Beta strandi98 – 1069Combined sources
    Turni108 – 1103Combined sources
    Beta strandi119 – 1268Combined sources
    Helixi128 – 1325Combined sources
    Helixi135 – 14713Combined sources
    Beta strandi149 – 16012Combined sources
    Helixi162 – 17110Combined sources
    Beta strandi177 – 1826Combined sources
    Turni191 – 1933Combined sources
    Beta strandi196 – 2016Combined sources
    Beta strandi206 – 2116Combined sources
    Helixi215 – 2239Combined sources
    Turni224 – 2263Combined sources
    Beta strandi227 – 2348Combined sources
    Helixi235 – 24410Combined sources
    Helixi247 – 2515Combined sources
    Beta strandi252 – 2543Combined sources
    Helixi260 – 2667Combined sources
    Beta strandi269 – 2768Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RI1X-ray2.50A1-283[»]
    1RI2X-ray2.70A1-283[»]
    1RI3X-ray2.50A1-283[»]
    1RI4X-ray2.40A1-283[»]
    1RI5X-ray2.10A1-283[»]
    1Z3CX-ray2.20A1-283[»]
    2HV9X-ray2.60A1-283[»]
    ProteinModelPortaliQ8SR66.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8SR66.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 283283mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 362mRNA cap binding
    Regioni107 – 1082S-adenosyl-L-methionine binding
    Regioni125 – 1273S-adenosyl-L-methionine binding

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.PROSITE-ProRule annotation
    Contains 1 mRNA cap 0 methyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG1975. Eukaryota.
    ENOG410Y7HG. LUCA.
    HOGENOMiHOG000242614.
    InParanoidiQ8SR66.
    KOiK00565.
    OrthoDBiEOG7MWH6S.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR016899. mRNA_G-N7_MeTrfase.
    IPR004971. mRNA_G-N7_MeTrfase_dom.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PfamiPF03291. Pox_MCEL. 1 hit.
    [Graphical view]
    PIRSFiPIRSF028762. ABD1. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51562. RNA_CAP0_MT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8SR66-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEGKKEEIRE HYNSIRERGR ESRQRSKTIN IRNANNFIKA CLIRLYTKRG
    60 70 80 90 100
    DSVLDLGCGK GGDLLKYERA GIGEYYGVDI AEVSINDARV RARNMKRRFK
    110 120 130 140 150
    VFFRAQDSYG RHMDLGKEFD VISSQFSFHY AFSTSESLDI AQRNIARHLR
    160 170 180 190 200
    PGGYFIMTVP SRDVILERYK QGRMSNDFYK IELEKMEDVP MESVREYRFT
    210 220 230 240 250
    LLDSVNNCIE YFVDFTRMVD GFKRLGLSLV ERKGFIDFYE DEGRRNPELS
    260 270 280
    KKMGLGCLTR EESEVVGIYE VVVFRKLVPE SDA
    Length:283
    Mass (Da):33,074
    Last modified:May 29, 2013 - v2
    Checksum:i40ABA7B1522C7001
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL590449 Genomic DNA. Translation: CAD25757.2.
    RefSeqiNP_586153.1. NM_001041986.1.

    Genome annotation databases

    EnsemblFungiiCAD25757; CAD25757; CAD25757.
    GeneIDi859802.
    KEGGiecu:ECU10_0380.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL590449 Genomic DNA. Translation: CAD25757.2.
    RefSeqiNP_586153.1. NM_001041986.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RI1X-ray2.50A1-283[»]
    1RI2X-ray2.70A1-283[»]
    1RI3X-ray2.50A1-283[»]
    1RI4X-ray2.40A1-283[»]
    1RI5X-ray2.10A1-283[»]
    1Z3CX-ray2.20A1-283[»]
    2HV9X-ray2.60A1-283[»]
    ProteinModelPortaliQ8SR66.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi284813.NP_586153.1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiCAD25757; CAD25757; CAD25757.
    GeneIDi859802.
    KEGGiecu:ECU10_0380.

    Organism-specific databases

    EuPathDBiMicrosporidiaDB:ECU10_0380.

    Phylogenomic databases

    eggNOGiKOG1975. Eukaryota.
    ENOG410Y7HG. LUCA.
    HOGENOMiHOG000242614.
    InParanoidiQ8SR66.
    KOiK00565.
    OrthoDBiEOG7MWH6S.

    Enzyme and pathway databases

    BRENDAi2.1.1.56. 7412.

    Miscellaneous databases

    EvolutionaryTraceiQ8SR66.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR016899. mRNA_G-N7_MeTrfase.
    IPR004971. mRNA_G-N7_MeTrfase_dom.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PfamiPF03291. Pox_MCEL. 1 hit.
    [Graphical view]
    PIRSFiPIRSF028762. ABD1. 1 hit.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51562. RNA_CAP0_MT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: GB-M1.
    2. "Identification of transcriptional signals in Encephalitozoon cuniculi widespread among Microsporidia phylum: support for accurate structural genome annotation."
      Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P., Cornman R.S., Evans J.D., Delbac F., Peyret P.
      BMC Genomics 10:607-607(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: GB-M1.
    3. "Structure and mechanism of mRNA cap (guanine-N7) methyltransferase."
      Fabrega C., Hausmann S., Shen V., Shuman S., Lima C.D.
      Mol. Cell 13:77-89(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES, MUTAGENESIS OF ARG-32; ASN-35; ASN-36; LYS-39; LYS-60; ASP-63; LYS-66; ASP-79; ILE-80; ARG-91; 107-ASP-SER-108; TYR-109; PHE-126; LEU-201 AND TYR-269.
    4. "Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition by S-adenosylmethionine analogs, and structure-guided mutational analysis."
      Hausmann S., Zheng S., Fabrega C., Schneller S.W., Lima C.D., Shuman S.
      J. Biol. Chem. 280:20404-20412(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-39; ASP-55; ASP-63 AND ASP-79.
    5. "Mutational analysis of Encephalitozoon cuniculi mRNA cap (guanine-N7) methyltransferase, structure of the enzyme bound to sinefungin, and evidence that cap methyltransferase is the target of sinefungin's antifungal activity."
      Zheng S., Hausmann S., Liu Q., Ghosh A., Schwer B., Lima C.D., Shuman S.
      J. Biol. Chem. 281:35904-35913(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, MUTAGENESIS OF ASN-36; LYS-39; ASP-55; LYS-60; ASP-63; LYS-66; ASP-79; ARG-91; TYR-109; PHE-126; HIS-129; TYR-130 AND GLU-210.

    Entry informationi

    Entry nameiMCES_ENCCU
    AccessioniPrimary (citable) accession number: Q8SR66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: May 29, 2013
    Last modified: November 11, 2015
    This is version 79 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.