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Protein

mRNA cap guanine-N7 methyltransferase

Gene

rnmt

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC.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 sitei107 – 1071S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei131 – 1311S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Sitei134 – 1341mRNA cap bindingPROSITE-ProRule annotation
Sitei140 – 1401mRNA cap bindingPROSITE-ProRule annotation
Binding sitei153 – 1531S-adenosyl-L-methioninePROSITE-ProRule annotation
Sitei165 – 1651mRNA cap bindingPROSITE-ProRule annotation
Binding sitei214 – 2141mRNA capPROSITE-ProRule annotation
Binding sitei296 – 2961mRNA capPROSITE-ProRule annotation
Binding sitei393 – 3931mRNA capPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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

BRENDAi2.1.1.56. 6725.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA cap guanine-N7 methyltransferase (EC:2.1.1.56)
Alternative name(s):
RG7MT1
mRNA (guanine-N(7)-)-methyltransferase
mRNA cap methyltransferase
Short name:
xCMT1
Gene namesi
Name:rnmt
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-944374. rnmt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 402402mRNA cap guanine-N7 methyltransferasePRO_0000248326Add
BLAST

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Expression decreases after gastrulation.1 Publication

Interactioni

Protein-protein interaction databases

IntActiQ9I8S2. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9I8S2.
SMRiQ9I8S2. Positions 96-401.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 402348mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni103 – 1042mRNA cap bindingPROSITE-ProRule annotation
Regioni187 – 1882S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni210 – 2123S-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

HOVERGENiHBG081963.
KOiK00565.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
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.

Q9I8S2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHVLNPEEK VSQTNSESGG ADGAFQHVKG EHSSPKLSAS EKSLPGNTKS
60 70 80 90 100
PLKRKAAEPD SPPKRPRLEE GHGSLVVTHY NELPETGLEI RSQSRIFHLR
110 120 130 140 150
NFNNWMKSAL IGEFVEKVQQ RTRNITVLDL GCGKGGDLLK WRKGGISKLV
160 170 180 190 200
CTDIADVSVK QCEQRYKDMK RKSRNERIFE AEFLTSDSTK ELLSEKYIDP
210 220 230 240 250
EIKFDICSCQ FVYHYSFETY EQADTMLRNA CERLCPGGFF IGTTPDGFEL
260 270 280 290 300
VKRLEASDTN SFGNDVYTVT FEKKGKYPLF GCKYDFSLEE VVNVPEFLVY
310 320 330 340 350
FPVLVEMAKK YQMKLIYKKT FREFFEEKVK NDEQKMLLKR MKALESYPAA
360 370 380 390 400
PNTKLVSGRT EDYEHAQKMV ENGQIKLPLG TLSKSEWDAT SIYLLFAFEK

QA
Length:402
Mass (Da):46,003
Last modified:October 1, 2000 - v1
Checksum:i5370C6C956FD0E07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061M → I in AAH94147 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218795 mRNA. Translation: AAF43145.1.
BC094147 mRNA. Translation: AAH94147.1.
PIRiJC7199.
RefSeqiNP_001082004.1. NM_001088535.1.
UniGeneiXl.649.

Genome annotation databases

GeneIDi398173.
KEGGixla:398173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF218795 mRNA. Translation: AAF43145.1.
BC094147 mRNA. Translation: AAH94147.1.
PIRiJC7199.
RefSeqiNP_001082004.1. NM_001088535.1.
UniGeneiXl.649.

3D structure databases

ProteinModelPortaliQ9I8S2.
SMRiQ9I8S2. Positions 96-401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9I8S2. 1 interaction.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398173.
KEGGixla:398173.

Organism-specific databases

CTDi8731.
XenbaseiXB-GENE-944374. rnmt.

Phylogenomic databases

HOVERGENiHBG081963.
KOiK00565.

Enzyme and pathway databases

BRENDAi2.1.1.56. 6725.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
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_XENLA
AccessioniPrimary (citable) accession number: Q9I8S2
Secondary accession number(s): Q52KX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.