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Protein

mRNA cap guanine-N7 methyltransferase

Gene

ABD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for methylating the 5'-cap structure of mRNAs.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei154 – 1541S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei172 – 1721S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei175 – 1751mRNA cap bindingPROSITE-ProRule annotation
Sitei181 – 1811mRNA cap bindingPROSITE-ProRule annotation
Binding sitei194 – 1941S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei206 – 2061mRNA cap bindingPROSITE-ProRule annotation
Binding sitei253 – 2531mRNA capPROSITE-ProRule annotation
Binding sitei347 – 3471mRNA capPROSITE-ProRule annotation
Binding sitei416 – 4161mRNA capPROSITE-ProRule annotation

GO - Molecular functioni

  • mRNA (guanine-N7-)-methyltransferase activity Source: SGD
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: SGD
  • RNA (guanine-N7)-methylation Source: GOC
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

BioCyciMetaCyc:G3O-29167-MONOMER.
YEAST:G3O-29167-MONOMER.
BRENDAi2.1.1.56. 984.
ReactomeiR-SCE-72086. mRNA Capping.
R-SCE-77075. RNA Pol II CTD phosphorylation and interaction with CE.

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:YBR236C
ORF Names:YBR1602
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR236C.
SGDiS000000440. ABD1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681V → A: Still viable; normal growth. 1 Publication
Mutagenesisi170 – 1701E → A: Non-viable; reduced enzyme activity to 8% of wild-type. 2 Publications
Mutagenesisi170 – 1701E → D: Still viable; increase in activity. 2 Publications
Mutagenesisi170 – 1701E → Q: Non-viable; reduced enzyme activity to 8% of wild-type. 2 Publications
Mutagenesisi172 – 1721G → A: Still viable; normal growth. 1 Publication
Mutagenesisi174 – 1741G → A: Non viable; no growth. 1 Publication
Mutagenesisi176 – 1761G → A: Still viable; normal growth. 1 Publication
Mutagenesisi178 – 1781D → A: Microcolony formation. 1 Publication
Mutagenesisi181 – 1811K → A: Still viable; normal growth. 1 Publication
Mutagenesisi182 – 1821Y → A: Still viable; normal growth. 1 Publication
Mutagenesisi194 – 1941D → A: Lethal; no enzyme activity. 2 Publications
Mutagenesisi194 – 1941D → E: Still viable; activity near to wild-type. 2 Publications
Mutagenesisi194 – 1941D → N: Lethal; no enzyme activity. 2 Publications
Mutagenesisi206 – 2061R → A: Lethal. 2 Publications
Mutagenesisi206 – 2061R → K: Still viable; little change in enzyme activity. 2 Publications
Mutagenesisi253 – 2531H → A: Still viable; normal growth. 1 Publication
Mutagenesisi254 – 2541Y → A: Non viable; no growth. 2 Publications
Mutagenesisi254 – 2541Y → F: Still viable; slow growth; near to wild-type enzyme activity. 2 Publications
Mutagenesisi254 – 2541Y → S: Lethal; Enzyme activity 10% of wild-type. 2 Publications
Mutagenesisi276 – 2761G → A: Still viable; normal growth. 1 Publication
Mutagenesisi277 – 2771G → A: Still viable; normal growth. 1 Publication
Mutagenesisi282 – 2821T → A: Still viable; normal growth. 1 Publication
Mutagenesisi287 – 2871E → A: Still viable; normal growth. 1 Publication
Mutagenesisi347 – 3471E → A: Still viable; normal growth. 1 Publication
Mutagenesisi348 – 3481Y → A: Still viable; normal growth. 1 Publication
Mutagenesisi349 – 3491V → A: Still viable; normal growth. 1 Publication
Mutagenesisi350 – 3501V → A: Still viable; normal growth. 1 Publication
Mutagenesisi361 – 3611E → A: Still viable; normal growth. 1 Publication
Mutagenesisi362 – 3621Y → A: Still viable; normal growth. 1 Publication
Mutagenesisi363 – 3631G → A: Still viable; normal growth. 1 Publication
Mutagenesisi366 – 3661L → A: Still viable; normal growth. 1 Publication
Mutagenesisi367 – 3671V → A: Still viable; normal growth. 1 Publication
Mutagenesisi372 – 3721F → A: Still viable; normal growth. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436mRNA cap guanine-N7 methyltransferasePRO_0000210134Add
BLAST

Proteomic databases

MaxQBiP32783.
PeptideAtlasiP32783.

PTM databases

iPTMnetiP32783.

Interactioni

Protein-protein interaction databases

BioGridi32931. 128 interactions.
DIPiDIP-2503N.
IntActiP32783. 10 interactions.
MINTiMINT-631955.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IC3model-A140-424[»]
ProteinModelPortaliP32783.
SMRiP32783. Positions 141-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 430330mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 1512mRNA cap bindingPROSITE-ProRule annotation
Regioni223 – 2242S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni249 – 2513S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

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

GeneTreeiENSGT00390000002368.
HOGENOMiHOG000242614.
InParanoidiP32783.
KOiK00565.
OMAiCFGESLG.
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.

P32783-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKPEKPIW MSQEDYDRQY GSITGDESST VSKKDSKVTA NAPGDGNGSL
60 70 80 90 100
PVLQSSSILT SKVSDLPIEA ESGFKIQKRR HERYDQEERL RKQRAQKLRE
110 120 130 140 150
EQLKRHEIEM TANRSINVDQ IVREHYNERT IIANRAKRNL SPIIKLRNFN
160 170 180 190 200
NAIKYMLIDK YTKPGDVVLE LGCGKGGDLR KYGAAGISQF IGIDISNASI
210 220 230 240 250
QEAHKRYRSM RNLDYQVVLI TGDCFGESLG VAVEPFPDCR FPCDIVSTQF
260 270 280 290 300
CLHYAFETEE KARRALLNVA KSLKIGGHFF GTIPDSEFIR YKLNKFPKEV
310 320 330 340 350
EKPSWGNSIY KVTFENNSYQ KNDYEFTSPY GQMYTYWLED AIDNVPEYVV
360 370 380 390 400
PFETLRSLAD EYGLELVSQM PFNKFFVQEI PKWIERFSPK MREGLQRSDG
410 420 430
RYGVEGDEKE AASYFYTMFA FRKVKQYIEP ESVKPN
Length:436
Mass (Da):50,341
Last modified:October 1, 1993 - v1
Checksum:iEA5A68F0C4A57C4C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1261Y → C in AAT92789 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12000 Genomic DNA. Translation: AAA34383.1.
Z36105 Genomic DNA. Translation: CAA85199.1.
AY692770 Genomic DNA. Translation: AAT92789.1.
BK006936 Genomic DNA. Translation: DAA07352.1.
PIRiS41782.
RefSeqiNP_009795.3. NM_001178584.3.

Genome annotation databases

EnsemblFungiiYBR236C; YBR236C; YBR236C.
GeneIDi852538.
KEGGisce:YBR236C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12000 Genomic DNA. Translation: AAA34383.1.
Z36105 Genomic DNA. Translation: CAA85199.1.
AY692770 Genomic DNA. Translation: AAT92789.1.
BK006936 Genomic DNA. Translation: DAA07352.1.
PIRiS41782.
RefSeqiNP_009795.3. NM_001178584.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IC3model-A140-424[»]
ProteinModelPortaliP32783.
SMRiP32783. Positions 141-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32931. 128 interactions.
DIPiDIP-2503N.
IntActiP32783. 10 interactions.
MINTiMINT-631955.

PTM databases

iPTMnetiP32783.

Proteomic databases

MaxQBiP32783.
PeptideAtlasiP32783.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR236C; YBR236C; YBR236C.
GeneIDi852538.
KEGGisce:YBR236C.

Organism-specific databases

EuPathDBiFungiDB:YBR236C.
SGDiS000000440. ABD1.

Phylogenomic databases

GeneTreeiENSGT00390000002368.
HOGENOMiHOG000242614.
InParanoidiP32783.
KOiK00565.
OMAiCFGESLG.
OrthoDBiEOG7MWH6S.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29167-MONOMER.
YEAST:G3O-29167-MONOMER.
BRENDAi2.1.1.56. 984.
ReactomeiR-SCE-72086. mRNA Capping.
R-SCE-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

PROiP32783.

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. "Molecular analysis of the ABD1 gene of Saccharomyces cerevisiae, a gene that displays mutational synergism with the bud formation gene BEM1."
    Corrado K., Pringle J.R.
    Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded by an essential gene."
    Mao X., Schwer B., Shuman S.
    Mol. Cell. Biol. 15:4167-4174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: cap methyltransferase activity is essential for cell growth."
    Mao X., Schwer B., Shuman S.
    Mol. Cell. Biol. 16:475-480(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-174; ASP-178; HIS-253; TYR-254; THR-282; GLU-287; GLU-361 AND TYR-362.
  7. "Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae."
    Wang S.P., Shuman S.
    J. Biol. Chem. 272:14683-14689(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-168; GLU-170; GLY-172; GLY-176; LYS-181; TYR-182; ASP-194; ARG-206; TYR-254; GLY-276; GLY-277; GLU-347; TYR-348; VAL-349; VAL-350; GLY-363; LEU-366; VAL-367 AND PHE-372.
  8. "Dynamic association of capping enzymes with transcribing RNA polymerase II."
    Schroeder S.C., Schwer B., Shuman S., Bentley D.
    Genes Dev. 14:2435-2440(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "mRNA:guanine-N7 cap methyltransferases: identification of novel members of the family, evolutionary analysis, homology modeling, and analysis of sequence-structure-function relationships."
    Bujnicki J.M., Feder M., Radlinska M., Rychlewski L.
    BMC Bioinformatics 2:2-2(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 140-424, MUTAGENESIS OF GLU-170; ASP-194 AND ARG-206.

Entry informationi

Entry nameiMCES_YEAST
AccessioniPrimary (citable) accession number: P32783
Secondary accession number(s): D6VQN2, Q6B2G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 136 of the entry and version 1 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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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.