UniProtKB - P32783 (MCES_YEAST)
Protein
mRNA cap guanine-N7 methyltransferase
Gene
ABD1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Responsible for methylating the 5'-cap structure of mRNAs.1 Publication
Catalytic activityi
- a 5'-end (5'-triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-guanosine in mRNA + S-adenosyl-L-homocysteinePROSITE-ProRule annotationBy similarityEC:2.1.1.56PROSITE-ProRule annotationBy similarity
- a 5'-end (5'-triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-adenosine in mRNA + S-adenosyl-L-homocysteinePROSITE-ProRule annotationBy similarityEC:2.1.1.56PROSITE-ProRule annotationBy similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 154 | S-adenosyl-L-methioninePROSITE-ProRule annotation | 1 | |
Binding sitei | 172 | S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation | 1 | |
Sitei | 175 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Sitei | 181 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Binding sitei | 194 | S-adenosyl-L-methioninePROSITE-ProRule annotation | 1 | |
Sitei | 206 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Binding sitei | 223 | S-adenosyl-L-methionine; via amide nitrogenBy similarity | 1 | |
Binding sitei | 249 | S-adenosyl-L-methionine; via carbonyl oxygenBy similarity | 1 | |
Sitei | 253 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Binding sitei | 254 | S-adenosyl-L-methionineBy similarity | 1 | |
Sitei | 347 | mRNA cap bindingPROSITE-ProRule annotation | 1 | |
Sitei | 416 | mRNA cap bindingPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- mRNA (guanine-N7-)-methyltransferase activity Source: SGD
- RNA binding Source: UniProtKB-KW
GO - Biological processi
- 7-methylguanosine mRNA capping Source: SGD
Keywordsi
Molecular function | Methyltransferase, RNA-binding, Transferase |
Biological process | mRNA capping, mRNA processing |
Ligand | S-adenosyl-L-methionine |
Enzyme and pathway databases
BioCyci | MetaCyc:G3O-29167-MONOMER |
BRENDAi | 2.1.1.56, 984 |
Reactomei | R-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:2.1.1.56By similarity)Alternative name(s): mRNA (guanine-N(7)-)-methyltransferase mRNA cap methyltransferase |
Gene namesi | Name:ABD1 Ordered Locus Names:YBR236C ORF Names:YBR1602 |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
EuPathDBi | FungiDB:YBR236C |
SGDi | S000000440, ABD1 |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Cytosol
- cytosol Source: SGD
Nucleus
- nucleus Source: SGD
Other locations
- mRNA cap binding complex Source: GO_Central
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 168 | V → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 170 | E → A: Non-viable; reduced enzyme activity to 8% of wild-type. 2 Publications | 1 | |
Mutagenesisi | 170 | E → D: Still viable; increase in activity. 2 Publications | 1 | |
Mutagenesisi | 170 | E → Q: Non-viable; reduced enzyme activity to 8% of wild-type. 2 Publications | 1 | |
Mutagenesisi | 172 | G → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 174 | G → A: Non viable; no growth. 1 Publication | 1 | |
Mutagenesisi | 176 | G → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 178 | D → A: Microcolony formation. 1 Publication | 1 | |
Mutagenesisi | 181 | K → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 182 | Y → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 194 | D → A: Lethal; no enzyme activity. 2 Publications | 1 | |
Mutagenesisi | 194 | D → E: Still viable; activity near to wild-type. 2 Publications | 1 | |
Mutagenesisi | 194 | D → N: Lethal; no enzyme activity. 2 Publications | 1 | |
Mutagenesisi | 206 | R → A: Lethal. 2 Publications | 1 | |
Mutagenesisi | 206 | R → K: Still viable; little change in enzyme activity. 2 Publications | 1 | |
Mutagenesisi | 253 | H → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 254 | Y → A: Non viable; no growth. 2 Publications | 1 | |
Mutagenesisi | 254 | Y → F: Still viable; slow growth; near to wild-type enzyme activity. 2 Publications | 1 | |
Mutagenesisi | 254 | Y → S: Lethal; Enzyme activity 10% of wild-type. 2 Publications | 1 | |
Mutagenesisi | 276 | G → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 277 | G → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 282 | T → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 287 | E → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 347 | E → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 348 | Y → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 349 | V → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 350 | V → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 361 | E → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 362 | Y → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 363 | G → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 366 | L → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 367 | V → A: Still viable; normal growth. 1 Publication | 1 | |
Mutagenesisi | 372 | F → A: Still viable; normal growth. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000210134 | 1 – 436 | mRNA cap guanine-N7 methyltransferaseAdd BLAST | 436 |
Proteomic databases
MaxQBi | P32783 |
PaxDbi | P32783 |
PRIDEi | P32783 |
PTM databases
iPTMneti | P32783 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 32931, 344 interactors |
DIPi | DIP-2503N |
IntActi | P32783, 10 interactors |
MINTi | P32783 |
STRINGi | 4932.YBR236C |
Miscellaneous databases
RNActi | P32783, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 101 – 430 | mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd BLAST | 330 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 150 – 151 | mRNA cap bindingPROSITE-ProRule annotation | 2 |
Sequence similaritiesi
Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.PROSITE-ProRule annotation
Phylogenomic databases
eggNOGi | KOG1975, Eukaryota |
GeneTreei | ENSGT00390000002368 |
HOGENOMi | CLU_020346_2_0_1 |
InParanoidi | P32783 |
OMAi | EFFACDS |
Family and domain databases
InterProi | View protein in InterPro IPR004971, mRNA_G-N7_MeTrfase_dom IPR016899, mRNA_G-N7_MeTrfase_euk IPR039753, RG7MT1 IPR029063, SAM-dependent_MTases |
PANTHERi | PTHR12189, PTHR12189, 1 hit |
Pfami | View protein in Pfam PF03291, Pox_MCEL, 1 hit |
PIRSFi | PIRSF028762, ABD1, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
PROSITEi | View protein in PROSITE PS51562, RNA_CAP0_MT, 1 hit |
i Sequence
Sequence statusi: Complete.
P32783-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 126 | Y → C in AAT92789 (PubMed:17322287).Curated | 1 |
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 |
PIRi | S41782 |
RefSeqi | NP_009795.3, NM_001178584.3 |
Genome annotation databases
EnsemblFungii | YBR236C_mRNA; YBR236C; YBR236C |
GeneIDi | 852538 |
KEGGi | sce:YBR236C |
Similar proteinsi
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 |
PIRi | S41782 |
RefSeqi | NP_009795.3, NM_001178584.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1IC3 | model | - | A | 140-424 | [»] | |
SMRi | P32783 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 32931, 344 interactors |
DIPi | DIP-2503N |
IntActi | P32783, 10 interactors |
MINTi | P32783 |
STRINGi | 4932.YBR236C |
PTM databases
iPTMneti | P32783 |
Proteomic databases
MaxQBi | P32783 |
PaxDbi | P32783 |
PRIDEi | P32783 |
Genome annotation databases
EnsemblFungii | YBR236C_mRNA; YBR236C; YBR236C |
GeneIDi | 852538 |
KEGGi | sce:YBR236C |
Organism-specific databases
EuPathDBi | FungiDB:YBR236C |
SGDi | S000000440, ABD1 |
Phylogenomic databases
eggNOGi | KOG1975, Eukaryota |
GeneTreei | ENSGT00390000002368 |
HOGENOMi | CLU_020346_2_0_1 |
InParanoidi | P32783 |
OMAi | EFFACDS |
Enzyme and pathway databases
BioCyci | MetaCyc:G3O-29167-MONOMER |
BRENDAi | 2.1.1.56, 984 |
Reactomei | R-SCE-72086, mRNA Capping R-SCE-77075, RNA Pol II CTD phosphorylation and interaction with CE |
Miscellaneous databases
PROi | PR:P32783 |
RNActi | P32783, protein |
Family and domain databases
InterProi | View protein in InterPro IPR004971, mRNA_G-N7_MeTrfase_dom IPR016899, mRNA_G-N7_MeTrfase_euk IPR039753, RG7MT1 IPR029063, SAM-dependent_MTases |
PANTHERi | PTHR12189, PTHR12189, 1 hit |
Pfami | View protein in Pfam PF03291, Pox_MCEL, 1 hit |
PIRSFi | PIRSF028762, ABD1, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
PROSITEi | View protein in PROSITE PS51562, RNA_CAP0_MT, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MCES_YEAST | |
Accessioni | P32783Primary (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: | December 2, 2020 | |
This is version 170 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome II
Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names