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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)DescriptionActionsGraphical viewLength
    Binding sitei39S-adenosyl-L-methionine1
    Binding sitei57S-adenosyl-L-methionine; via carbonyl oxygen1
    Sitei60mRNA cap binding1
    Sitei66mRNA cap binding1
    Binding sitei79S-adenosyl-L-methionine1
    Sitei91mRNA cap binding1
    Binding sitei129mRNA cap1
    Binding sitei210mRNA cap1
    Binding sitei269mRNA cap1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi32R → A: No effect. Loss of activity; when associated with A-60. 1 Publication1
    Mutagenesisi35N → A: No effect. Loss of activity; when associated with A-269. 1 Publication1
    Mutagenesisi36N → A: Reduces activity by 85%. 2 Publications1
    Mutagenesisi36N → D: Reduces activity by 96%. 2 Publications1
    Mutagenesisi39K → A, Q or R: Loss of activity. 3 Publications1
    Mutagenesisi55D → A or N: Reduces activity by 95%. 2 Publications1
    Mutagenesisi55D → E: Reduces activity by 60%. 2 Publications1
    Mutagenesisi60K → A: Reduces activity by 92%. Loss of activity; when associated with A-32. 2 Publications1
    Mutagenesisi63D → A or N: Reduces activity by 99%. 3 Publications1
    Mutagenesisi63D → E: Reduces activity by 75%. 3 Publications1
    Mutagenesisi66K → A: Reduces activity by 80%. 2 Publications1
    Mutagenesisi66K → Q or R: Reduces activity by 90%. 2 Publications1
    Mutagenesisi79D → A or N: Loss of activity. 3 Publications1
    Mutagenesisi79D → E: Reduces activity by 77%. 3 Publications1
    Mutagenesisi80I → A: No effect. Strongly reduced activity; when associated with A-109. 1 Publication1
    Mutagenesisi91R → A or Q: Reduces activity by over 98%. 2 Publications1
    Mutagenesisi91R → K: Reduces activity by 96%. 2 Publications1
    Mutagenesisi107 – 108DS → AA: Slightly reduced activity. 1 Publication2
    Mutagenesisi109Y → A: Reduces activity by 83%. Strongly reduced activity; when associated with A-80. 2 Publications1
    Mutagenesisi126F → A or N: Loss of activity. 2 Publications1
    Mutagenesisi126F → H: Reduces activity by 92%. 2 Publications1
    Mutagenesisi126F → I: Reduces activity by 75%. 2 Publications1
    Mutagenesisi126F → L: Reduces activity by 55%. 2 Publications1
    Mutagenesisi126F → V: Reduces activity by 84%. 2 Publications1
    Mutagenesisi129H → A: Reduces activity by 53%. Reduces activity by 99%; when associated with L-130. 1 Publication1
    Mutagenesisi130Y → A, S or V: Reduces activity by 98%. 1 Publication1
    Mutagenesisi130Y → F: Reduces activity by 66%. 1 Publication1
    Mutagenesisi130Y → L: Reduces activity by 99%; when associated with A-129. 1 Publication1
    Mutagenesisi201L → A: No effect. 1 Publication1
    Mutagenesisi210E → A: Reduces activity by 87%. 1 Publication1
    Mutagenesisi269Y → A: Reduced activity. Loss of activity; when associated with A-35. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002101421 – 283mRNA cap guanine-N7 methyltransferaseAdd BLAST283

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi284813.NP_586153.1.

    Structurei

    Secondary structure

    1283
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi29 – 46Combined sources18
    Beta strandi52 – 56Combined sources5
    Turni59 – 63Combined sources5
    Helixi64 – 70Combined sources7
    Beta strandi73 – 80Combined sources8
    Helixi82 – 93Combined sources12
    Beta strandi98 – 106Combined sources9
    Turni108 – 110Combined sources3
    Beta strandi119 – 126Combined sources8
    Helixi128 – 132Combined sources5
    Helixi135 – 147Combined sources13
    Beta strandi149 – 160Combined sources12
    Helixi162 – 171Combined sources10
    Beta strandi177 – 182Combined sources6
    Turni191 – 193Combined sources3
    Beta strandi196 – 201Combined sources6
    Beta strandi206 – 211Combined sources6
    Helixi215 – 223Combined sources9
    Turni224 – 226Combined sources3
    Beta strandi227 – 234Combined sources8
    Helixi235 – 244Combined sources10
    Helixi247 – 251Combined sources5
    Beta strandi252 – 254Combined sources3
    Helixi260 – 266Combined sources7
    Beta strandi269 – 276Combined sources8

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    SMRiQ8SR66.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8SR66.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini1 – 283mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd BLAST283

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni35 – 36mRNA cap binding2
    Regioni107 – 108S-adenosyl-L-methionine binding2
    Regioni125 – 127S-adenosyl-L-methionine binding3

    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.
    OrthoDBiEOG092C2SMS.

    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
    PDB 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.
    SMRiQ8SR66.
    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.
    OrthoDBiEOG092C2SMS.

    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...

    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 2, 2016
    This is version 81 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.