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Protein

Protein arginine N-methyltransferase 2

Gene

RMT2

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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. Monomethylates ribosomal protein L12.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei193 – 1931S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei223 – 2231S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei315 – 3151S-adenosyl-L-methioninePROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 2By similarity (EC:2.1.1.-By similarity)
Alternative name(s):
Protein-arginine N5-methyltransferaseBy similarity
Type IV protein arginine N-methyltransferaseBy similarity
Short name:
Type IV PRMTBy similarity
Gene namesi
Name:RMT2By similarity
Ordered Locus Names:KLLA0E03531g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
Proteomesi
  • UP000000598 Componenti: Chromosome E

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407Protein arginine N-methyltransferase 2PRO_0000228977Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi284590.XP_454108.1.

Structurei

3D structure databases

ProteinModelPortaliQ6CPN1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini186 – 407222RMT2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni246 – 2516S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni267 – 2693S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni294 – 2952S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

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

eggNOGiKOG1709. Eukaryota.
ENOG4110T2S. LUCA.
HOGENOMiHOG000214351.
InParanoidiQ6CPN1.
KOiK18477.
OMAiICHADEI.
OrthoDBiEOG7CG78C.

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.

Q6CPN1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDLHHLLTF PERPISESSY LPELTRLLSA GIPATYTLEQ AAAFERGEEV
60 70 80 90 100
TEEDSNTTPL HILCRSLPSF EGSSKLSEDE ESVVLKLMDT LLEYGAGWNF
110 120 130 140 150
LDYENKHIGD LVLERKYPQD HCIYQRIVDA GVSAELLLRK IDGGEIEFIE
160 170 180 190 200
DPEDAATEAA TEAATEAEVI EGVTKGSEEA PFEDATAADQ ATYLKTDLEY
210 220 230 240 250
TDDALVTKEN RDGVMMDWET DIMSMAAKSL VSTRSTDECV VLNIGFGMGI
260 270 280 290 300
IDNFIQDEKV TKHYICEAHP DVLAKMKETG WFDKENVVIL EGRWQSRLNE
310 320 330 340 350
LLDQGEVFFD GIYYDTFSEH YQDMLDLYDV IVGLLKPEGT FSFFNGLGAD
360 370 380 390 400
RPVCYDVYRK IVELDVANYG MECRYQVINL RTLPNWNDVK RSYFNCTYYY

HPEIRFA
Length:407
Mass (Da):46,311
Last modified:August 16, 2004 - v1
Checksum:iEBE1C168834790D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382125 Genomic DNA. Translation: CAG99195.1.
RefSeqiXP_454108.1. XM_454108.1.

Genome annotation databases

EnsemblFungiiCAG99195; CAG99195; KLLA0_E03631g.
GeneIDi2894719.
KEGGikla:KLLA0E03631g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382125 Genomic DNA. Translation: CAG99195.1.
RefSeqiXP_454108.1. XM_454108.1.

3D structure databases

ProteinModelPortaliQ6CPN1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284590.XP_454108.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG99195; CAG99195; KLLA0_E03631g.
GeneIDi2894719.
KEGGikla:KLLA0E03631g.

Phylogenomic databases

eggNOGiKOG1709. Eukaryota.
ENOG4110T2S. LUCA.
HOGENOMiHOG000214351.
InParanoidiQ6CPN1.
KOiK18477.
OMAiICHADEI.
OrthoDBiEOG7CG78C.

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_KLULA
AccessioniPrimary (citable) accession number: Q6CPN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 72 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

Complete proteome, Reference proteome

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.