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Protein

Protein arginine N-methyltransferase 2

Gene

RMT2

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
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 sitei200 – 2001S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei230 – 2301S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei327 – 3271S-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:DEHA2E19228g
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
Proteomesi
  • UP000000599 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 – 434434Protein arginine N-methyltransferase 2PRO_0000228974Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6BNS9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini193 – 434242RMT2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni258 – 2636S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni279 – 2813S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni306 – 3072S-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

HOGENOMiHOG000214351.
InParanoidiQ6BNS9.
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.

Q6BNS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDLHELCGF QTRPIGPKYI EDLKFYLKNG IPATYTIEEA YNYTNNIEEE
60 70 80 90 100
PTTTTTPLHI ICSHIPNDAS NDEIDIINQM VEILLEYGAG WCLTDINDDT
110 120 130 140 150
PGCILIRRKL NNTPIYNQVV AAGVRAELLL RKVSEYDMEI IEDTDDLNHE
160 170 180 190 200
QFEGIQGEET TEEERKEEEP SNTSDIIDEQ KVEQPKEDLK EDPSSNQETY
210 220 230 240 250
LKTKLEYKDG ALVTKDRKDG VMMSWETDLM RMGCDSLFKG ASIDGEIDDE
260 270 280 290 300
VNILNIGFGM GIIDTMINNK NPTKQYICEA HPDVLAKLRL DGWYEKQNVV
310 320 330 340 350
ILEGRWQEQL NKLLSEGNVF FNGIYYDTYS EHYEDMLELF DIVVGILKPH
360 370 380 390 400
GVFSFFNGLG ADRQVVYEVY KQLVEMDLAN YGLICKFEQI EVPESTLQLE
410 420 430
VQNSTDNKSV WDDIKRAYWT CPTYYHPEAR FMDV
Length:434
Mass (Da):50,020
Last modified:August 16, 2004 - v1
Checksum:iFAB25B428C9824A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382137 Genomic DNA. Translation: CAG88414.1.
RefSeqiXP_460141.1. XM_460141.1.

Genome annotation databases

EnsemblFungiiCAG88414; CAG88414; DEHA2E19228g.
GeneIDi2902891.
KEGGidha:DEHA2E19228g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382137 Genomic DNA. Translation: CAG88414.1.
RefSeqiXP_460141.1. XM_460141.1.

3D structure databases

ProteinModelPortaliQ6BNS9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAG88414; CAG88414; DEHA2E19228g.
GeneIDi2902891.
KEGGidha:DEHA2E19228g.

Phylogenomic databases

HOGENOMiHOG000214351.
InParanoidiQ6BNS9.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiRMT2_DEBHA
AccessioniPrimary (citable) accession number: Q6BNS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: August 16, 2004
Last modified: September 7, 2016
This is version 70 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.