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UniProtKB/Swiss-Prot entry Q8SR66

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MCES_ENCCU
Primary accession number Q8SR66
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 2005
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 34)
Name and origin of the protein
Protein name mRNA cap guanine-N7 methyltransferase
Synonyms EC 2.1.1.56
mRNA (guanine-N(7)-)-methyltransferase
mRNA cap methyltransferase
Gene name
Name: ABD1
OrderedLocusNames: ECU10_0380
From
Encephalitozoon cuniculi [TaxID: 6035] 
Taxonomy Eukaryota; Fungi; Microsporidia; Unikaryonidae; Encephalitozoon.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GB-M1;
DOI=10.1038/35106579; PubMed=11719806 [NCBI, ExPASy, EBI, Israel, Japan]
Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P.;
"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi.";
Nature 414:450-453(2001).
[2]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES, AND MUTAGENESIS OF ARG-47; ASN-50; ASN-51; LYS-54; LYS-75; ASP-78; LYS-81; ASP-94; ILE-95; ARG-106; 122-ASP-SER-123; TYR-124; PHE-141; LEU-216 AND TYR-284.
DOI=10.1016/S1097-2765(03)00522-7; PubMed=14731396 [NCBI, ExPASy, EBI, Israel, Japan]
Fabrega C., Hausmann S., Shen V., Shuman S., Lima C.D.;
"Structure and mechanism of mRNA cap (guanine-N7) methyltransferase.";
Mol. Cell 13:77-89(2004).
[3]
 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF LYS-54; ASP-70; ASP-78 AND ASP-94.
DOI=10.1074/jbc.M501073200; PubMed=15760890 [NCBI, ExPASy, EBI, Israel, Japan]
Hausmann S., Zheng S., Fabrega C., Schneller S.W., Lima C.D., Shuman S.;
"Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition by S-adenosylmethionine analogs, and structure-guided mutational analysis.";
J. Biol. Chem. 280:20404-20412(2005).
[4]
 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, AND MUTAGENESIS OF ASN-51; LYS-54; ASP-70; LYS-75; ASP-78; LYS-81; ASP-94; ARG-106; TYR-124; PHE-141; HIS-144; TYR-145 AND GLU-225.
DOI=10.1074/jbc.M607292200; PubMed=16971388 [NCBI, ExPASy, EBI, Israel, Japan]
Zheng S., Hausmann S., Liu Q., Ghosh A., Schwer B., Lima C.D., Shuman S.;
"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.";
J. Biol. Chem. 281:35904-35913(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL590449; CAD25757.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_586153.1; -.
3D structure databases
PDB
1RI1; X-ray; 2.50 A; A=1-298.[ExPASy / RCSB / EBI]
1RI2; X-ray; 2.70 A; A=1-298.[ExPASy / RCSB / EBI]
1RI3; X-ray; 2.50 A; A=1-298.[ExPASy / RCSB / EBI]
1RI4; X-ray; 2.40 A; A=1-298.[ExPASy / RCSB / EBI]
1RI5; X-ray; 2.10 A; A=1-298.[ExPASy / RCSB / EBI]
1Z3C; X-ray; 2.20 A; A=1-298.[ExPASy / RCSB / EBI]
2HV9; X-ray; 2.60 A; A=1-298.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1RI1; -.
1RI2; -.
1RI3; -.
1RI4; -.
1RI5; -.
1Z3C; -.
2HV9; -.
ModBase Q8SR66.
Family and domain databases
InterPro IPR004971; Pox_MCEL.
Graphical view of domain structure.
Pfam PF03291; Pox_MCEL; 1.
Pfam graphical view of domain structure.
BLOCKS Q8SR66.
Genome annotation databases
GeneID 859802; -.
GenomeReviews AL590449_GR; ECU10_0380.
KEGG ecu:ECU10_0380; -.
NMPDR fig|6035.1.peg.1267; -.
Phylogenomic databases
HOGENOM Q8SR66; -.
Other
ProtoNet Q8SR66.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Methyltransferase; mRNA capping; mRNA processing; Nucleus; RNA-binding; S-adenosyl-L-methionine; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   298  298     mRNA cap guanine-N7 methyltransferase. PRO_0000210142
REGION   50    51  2     mRNA cap binding. 
REGION   122   123  2     S-adenosyl-L-methionine binding. 
REGION   140   142  3     S-adenosyl-L-methionine binding. 
BINDING   54    54        S-adenosyl-L-methionine. 
BINDING   72    72        S-adenosyl-L-methionine; via carbonyl oxygen. 
BINDING   75    75        mRNA cap. 
BINDING   81    81        mRNA cap. 
BINDING   94    94        S-adenosyl-L-methionine. 
BINDING   106   106        mRNA cap. 
BINDING   144   144        mRNA cap. 
BINDING   225   225        mRNA cap. 
BINDING   284   284        mRNA cap. 
MUTAGEN   47    47        R->A: No effect. Loss of activity; when associated with A-75. 
MUTAGEN   50    50        N->A: No effect. Loss of activity; when associated with A-284. 
MUTAGEN   51    51        N->A: Reduces activity by 85%. 
MUTAGEN   51    51        N->D: Reduces activity by 96%. 
MUTAGEN   54    54        K->A,Q,R: Loss of activity. 
MUTAGEN   70    70        D->A,N: Reduces activity by 95%. 
MUTAGEN   70    70        D->E: Reduces activity by 60%. 
MUTAGEN   75    75        K->A: Reduces activity by 92%. Loss of activity; when associated with A-47. 
MUTAGEN   78    78        D->A,N: Reduces activity by 99%. 
MUTAGEN   78    78        D->E: Reduces activity by 75%. 
MUTAGEN   81    81        K->A: Reduces activity by 80%. 
MUTAGEN   81    81        K->Q,R: Reduces activity by 90%. 
MUTAGEN   94    94        D->A,N: Loss of activity. 
MUTAGEN   94    94        D->E: Reduces activity by 77%. 
MUTAGEN   95    95        I->A: No effect. Strongly reduced activity; when associated with A-124. 
MUTAGEN   106   106        R->A,Q: Reduces activity by over 98%. 
MUTAGEN   106   106        R->K: Reduces activity by 96%. 
MUTAGEN   122   123        DS->AA: Slightly reduced activity. 
MUTAGEN   124   124        Y->A: Reduces activity by 83%. Strongly reduced activity; when associated with A-95. 
MUTAGEN   141   141        F->A,N: Loss of activity. 
MUTAGEN   141   141        F->H: Reduces activity by 92%. 
MUTAGEN   141   141        F->I: Reduces activity by 75%. 
MUTAGEN   141   141        F->L: Reduces activity by 55%. 
MUTAGEN   141   141        F->V: Reduces activity by 84%. 
MUTAGEN   144   144        H->A: Reduces activity by 53%. Reduces activity by 99%; when associated with L-145. 
MUTAGEN   145   145        Y->A,S,V: Reduces activity by 98%. 
MUTAGEN   145   145        Y->F: Reduces activity by 66%. 
MUTAGEN   216   216        L->A: No effect. 
MUTAGEN   225   225        E->A: Reduces activity by 87%. 
MUTAGEN   284   284        Y->A: Reduced activity. Loss of activity; when associated with A-50. 
HELIX   44    61  18      
STRAND   67    71  5      
TURN   74    78  5      
HELIX   79    85  7      
STRAND   88    95  8      
HELIX   97   108  12      
STRAND   114   121  8      
STRAND   123   126  4      
STRAND   134   141  8      
HELIX   143   146  4      
HELIX   150   161  12      
STRAND   164   175  12      
HELIX   177   186  10      
STRAND   192   197  6      
HELIX   206   208  3      
STRAND   211   216  6      
STRAND   221   226  6      
HELIX   230   239  10      
STRAND   242   249  8      
HELIX   250   260  11      
TURN   265   269  5      
HELIX   275   281  7      
STRAND   284   291  8      
Sequence information
Length: 298 AA [This is the length of the unprocessed precursor] Molecular weight: 34767 Da [This is the MW of the unprocessed precursor] CRC64: 03EF2775B7B6B062 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MDSSSPLKTF RKDQAMEGKK EEIREHYNSI RERGRESRQR SKTINIRNAN NFIKACLIRL 

        70         80         90        100        110        120 
YTKRGDSVLD LGCGKGGDLL KYERAGIGEY YGVDIAEVSI NDARVRARNM KRRFKVFFRA 

       130        140        150        160        170        180 
QDSYGRHMDL GKEFDVISSQ FSFHYAFSTS ESLDIAQRNI ARHLRPGGYF IMTVPSRDVI 

       190        200        210        220        230        240 
LERYKQGRMS NDFYKIELEK MEDVPMESVR EYRFTLLDSV NNCIEYFVDF TRMVDGFKRL 

       250        260        270        280        290 
GLSLVERKGF IDFYEDEGRR NPELSKKMGL GCLTREESEV VGIYEVVVFR KLVPESDA
Q8SR66 in FASTA format

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