Skip Header

Contribute Send feedback
Read comments (?) or add your own

P78587 (MCE1_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
mRNA-capping enzyme subunit alpha
Alternative name(s):
GTP--RNA guanylyltransferase
Short name=GTase
mRNA guanylyltransferase
EC=2.7.7.50
Gene names
Name:CGT1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate By similarity.

Catalytic activity

GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.

Subunit structure

The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the eukaryotic GTase family.

Ontologies

Keywords
   Biological processmRNA capping
mRNA processing
   Cellular componentNucleus
   LigandGTP-binding
Nucleotide-binding
   Molecular functionNucleotidyltransferase
Transferase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processmRNA capping

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmRNA cap methyltransferase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA guanylyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449mRNA-capping enzyme subunit alpha
PRO_0000210099

Regions

Compositional bias427 – 4359Poly-Gln

Sites

Active site671N6-GMP-lysine intermediate Potential

Secondary structure

1 ..................................................................... 449
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P78587 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: D93F44BF112305BB

FASTA44952,253
        10         20         30         40         50         60 
MIQLEEREIP VIPGNKLDEE ETKELRLMVA ELLGRRNTGF PGSQPVSFER RHLEETLMQK 

        70         80         90        100        110        120 
DYFVCEKTDG LRCLLFLIND PDKGEGVFLV TRENDYYFIP NIHFPLSVNE TREKPTYHHG 

       130        140        150        160        170        180 
TLLDGELVLE NRNVSEPVLR YVIFDALAIH GKCIIDRPLP KRLGYITENV MKPFDNFKKH 

       190        200        210        220        230        240 
NPDIVNSPEF PFKVGFKTML TSYHADDVLS KMDKLFHASD GLIYTCAETP YVFGTDQTLL 

       250        260        270        280        290        300 
KWKPAEENTV DFQLEFVFNE VQDPDLDERD PTSTYLDYDA KPNLIKLRVW QGSNVHTDFA 

       310        320        330        340        350        360 
KLDLSDDDWE RLKALEQPLQ GRIAECRQST TKKGYWEMLR FRNDKSNGNH ISVVEKILVS 

       370        380        390        400        410        420 
IKDGVKEKEV IEWCPKISRA WKKRENDRRQ KHFNGVARPA SVSHEEPLRK KIKTESNGNG 

       430        440 
HQTPPRQEQQ QQSQQILNDI PTYEDSDDE

« Hide

References

[1]"Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans."
Yamada-Okabe T., Shimmi O., Doi R., Mizumoto K., Arisawa M., Yamada-Okabe H.
Microbiology 142:2515-2523(1996) [PubMed: 8828219] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10259 / CBS 5796 / DSM 5817 / JCM 2078 / NBRC 1060.
[2]"Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II."
Fabrega C., Shen V., Shuman S., Lima C.D.
Mol. Cell 11:1549-1561(2003) [PubMed: 12820968] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D83180 Genomic DNA. Translation: BAA11833.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P16X-ray2.70A/B3-395[»]
ProteinModelPortalP78587.
SMRP78587. Positions 1-390.
ModBaseSearch...

Protein-protein interaction databases

STRINGP78587.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMAGSQPVSF.

Family and domain databases

InterProIPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR017075. mRNA_capping_enz_asu.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PfamPF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]
PIRSFPIRSF036959. mRNA_cap_alpha. 1 hit.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMCE1_CANAX
AccessionPrimary (citable) accession number: P78587
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: October 19, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents