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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)DescriptionActionsGraphical viewLength
Binding sitei154S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei172S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Sitei175mRNA cap bindingPROSITE-ProRule annotation1
Sitei181mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei194S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei206mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei253mRNA capPROSITE-ProRule annotation1
Binding sitei347mRNA capPROSITE-ProRule annotation1
Binding sitei416mRNA capPROSITE-ProRule annotation1

GO - Molecular functioni

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

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: SGD
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
  • mRNA cap binding complex Source: GO_Central
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi168V → A: Still viable; normal growth. 1 Publication1
Mutagenesisi170E → A: Non-viable; reduced enzyme activity to 8% of wild-type. 2 Publications1
Mutagenesisi170E → D: Still viable; increase in activity. 2 Publications1
Mutagenesisi170E → Q: Non-viable; reduced enzyme activity to 8% of wild-type. 2 Publications1
Mutagenesisi172G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi174G → A: Non viable; no growth. 1 Publication1
Mutagenesisi176G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi178D → A: Microcolony formation. 1 Publication1
Mutagenesisi181K → A: Still viable; normal growth. 1 Publication1
Mutagenesisi182Y → A: Still viable; normal growth. 1 Publication1
Mutagenesisi194D → A: Lethal; no enzyme activity. 2 Publications1
Mutagenesisi194D → E: Still viable; activity near to wild-type. 2 Publications1
Mutagenesisi194D → N: Lethal; no enzyme activity. 2 Publications1
Mutagenesisi206R → A: Lethal. 2 Publications1
Mutagenesisi206R → K: Still viable; little change in enzyme activity. 2 Publications1
Mutagenesisi253H → A: Still viable; normal growth. 1 Publication1
Mutagenesisi254Y → A: Non viable; no growth. 2 Publications1
Mutagenesisi254Y → F: Still viable; slow growth; near to wild-type enzyme activity. 2 Publications1
Mutagenesisi254Y → S: Lethal; Enzyme activity 10% of wild-type. 2 Publications1
Mutagenesisi276G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi277G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi282T → A: Still viable; normal growth. 1 Publication1
Mutagenesisi287E → A: Still viable; normal growth. 1 Publication1
Mutagenesisi347E → A: Still viable; normal growth. 1 Publication1
Mutagenesisi348Y → A: Still viable; normal growth. 1 Publication1
Mutagenesisi349V → A: Still viable; normal growth. 1 Publication1
Mutagenesisi350V → A: Still viable; normal growth. 1 Publication1
Mutagenesisi361E → A: Still viable; normal growth. 1 Publication1
Mutagenesisi362Y → A: Still viable; normal growth. 1 Publication1
Mutagenesisi363G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi366L → A: Still viable; normal growth. 1 Publication1
Mutagenesisi367V → A: Still viable; normal growth. 1 Publication1
Mutagenesisi372F → A: Still viable; normal growth. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002101341 – 436mRNA cap guanine-N7 methyltransferaseAdd BLAST436

Proteomic databases

MaxQBiP32783.
PRIDEiP32783.

PTM databases

iPTMnetiP32783.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini101 – 430mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd BLAST330

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 151mRNA cap bindingPROSITE-ProRule annotation2
Regioni223 – 224S-adenosyl-L-methionine bindingPROSITE-ProRule annotation2
Regioni249 – 251S-adenosyl-L-methionine bindingPROSITE-ProRule annotation3

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.
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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti126Y → C in AAT92789 (PubMed:17322287).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IC3model-A140-424[»]
ProteinModelPortaliP32783.
SMRiP32783.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP32783.

Proteomic databases

MaxQBiP32783.
PRIDEiP32783.

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.
OrthoDBiEOG092C2SMS.

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...

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: November 2, 2016
This is version 140 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.