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Protein

Protein arginine N-methyltransferase 2

Gene

RMT2

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

S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins (PubMed:9873020). Monomethylates ribosomal protein L12 (RPL12A/RPL12B) at 'Arg-67' (PubMed:11856739).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei196S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei226S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei319S-adenosyl-L-methioninePROSITE-ProRule annotation1

GO - Molecular functioni

  • protein-arginine N5-methyltransferase activity Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29993-MONOMER.
YEAST:G3O-29993-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 21 Publication (EC:2.1.1.-2 Publications)
Alternative name(s):
Protein-arginine N5-methyltransferase1 Publication
Type IV protein arginine N-methyltransferase1 Publication
Short name:
Type IV PRMT1 Publication
Gene namesi
Name:RMT21 Publication
Ordered Locus Names:YDR465CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR465C.
SGDiS000002873. RMT2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002289801 – 412Protein arginine N-methyltransferase 2Add BLAST412

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei181PhosphoserineCombined sources1
Modified residuei184PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03305.
PRIDEiQ03305.

PTM databases

iPTMnetiQ03305.

Interactioni

Subunit structurei

Monomer. Interacts with nucleoporins NUP49, NUP57 and NUP100.2 Publications

Protein-protein interaction databases

BioGridi32519. 22 interactors.
DIPiDIP-4490N.
IntActiQ03305. 3 interactors.
MINTiMINT-487758.

Structurei

3D structure databases

ProteinModelPortaliQ03305.
SMRiQ03305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini189 – 412RMT2PROSITE-ProRule annotationAdd BLAST224

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni250 – 255S-adenosyl-L-methionine bindingPROSITE-ProRule annotation6
Regioni271 – 273S-adenosyl-L-methionine bindingPROSITE-ProRule annotation3
Regioni298 – 299S-adenosyl-L-methionine bindingPROSITE-ProRule annotation2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.PROSITE-ProRule annotation
Contains 1 RMT2 (arginine N-methyltransferase 2-like) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000214351.
InParanoidiQ03305.
KOiK18477.
OMAiFEYGAGW.
OrthoDBiEOG092C2OT7.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR017408. Arginine_N-MeTrfase_2.
IPR026480. RMT2_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PIRSFiPIRSF038148. Arginine_N-mtfrase-2. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51559. SAM_RMT2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03305-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELHALLTF PERPISQSYY VPKLQHFLKS GIPATYTLEQ VAAFEHEEKN
60 70 80 90 100
RNGDKEFRES TDDNKTSNTT PLHVLARSLP LDIKDEELQV VMDMMNILFE
110 120 130 140 150
YGAGWNFIDY EDKTVGDLFL ERNQSRESPL YRRLVEAGVS AELLLRKLNG
160 170 180 190 200
GDVEFLDTDE LIGIEPEESV QTAVDGQKEE SVGSDDDATA ANQQVYLKTE
210 220 230 240 250
LEYKDDALIT KENKDGVMMD WETKIMELAS ETLFPDPEAT NSATILNIGF
260 270 280 290 300
GMGIIDTFIQ ARKPYRHYIC EAHPDVLAKM KMDGWYEKDN VVILEGRWQD
310 320 330 340 350
TLNNLLDKGE VFFDGIYYDT FSEHYQDILD LYDVVVGLIK PEGVFSFFNG
360 370 380 390 400
LGADRSLCYD VYKEIVEIDV ATYGMKCDYT RYSLDEQLPD WNDVKRSYFN
410
CNYYYHPRIT FA
Length:412
Mass (Da):47,469
Last modified:November 1, 1996 - v1
Checksum:i932B52EE4C4FFCF3
GO

Mass spectrometryi

Molecular mass is 47339±2 Da from positions 1 - 412. Determined by ESI. Measured from a recombinant protein expressed in E.coli.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33050 Genomic DNA. Translation: AAB64933.1.
BK006938 Genomic DNA. Translation: DAA12300.1.
PIRiS69633.
RefSeqiNP_010753.1. NM_001180773.1.

Genome annotation databases

EnsemblFungiiYDR465C; YDR465C; YDR465C.
GeneIDi852076.
KEGGisce:YDR465C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33050 Genomic DNA. Translation: AAB64933.1.
BK006938 Genomic DNA. Translation: DAA12300.1.
PIRiS69633.
RefSeqiNP_010753.1. NM_001180773.1.

3D structure databases

ProteinModelPortaliQ03305.
SMRiQ03305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32519. 22 interactors.
DIPiDIP-4490N.
IntActiQ03305. 3 interactors.
MINTiMINT-487758.

PTM databases

iPTMnetiQ03305.

Proteomic databases

MaxQBiQ03305.
PRIDEiQ03305.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR465C; YDR465C; YDR465C.
GeneIDi852076.
KEGGisce:YDR465C.

Organism-specific databases

EuPathDBiFungiDB:YDR465C.
SGDiS000002873. RMT2.

Phylogenomic databases

HOGENOMiHOG000214351.
InParanoidiQ03305.
KOiK18477.
OMAiFEYGAGW.
OrthoDBiEOG092C2OT7.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29993-MONOMER.
YEAST:G3O-29993-MONOMER.

Miscellaneous databases

PROiQ03305.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR017408. Arginine_N-MeTrfase_2.
IPR026480. RMT2_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PIRSFiPIRSF038148. Arginine_N-mtfrase-2. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51559. SAM_RMT2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRMT2_YEAST
AccessioniPrimary (citable) accession number: Q03305
Secondary accession number(s): D6VT90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.