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Protein

rRNA adenine N-6-methyltransferase

Gene

erm

Organism
Streptococcus pneumoniae
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.

Catalytic activityi

2 S-adenosyl-L-methionine + adenine(2085) in 23S rRNA = 2 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(2085) in 23S rRNA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei12 – 121S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei37 – 371S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation
Binding sitei58 – 581S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei83 – 831S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei100 – 1001S-adenosyl-L-methioninePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
rRNA adenine N-6-methyltransferase (EC:2.1.1.184)
Alternative name(s):
ErmAM
Macrolide-lincosamide-streptogramin B resistance protein
Gene namesi
Name:erm
OrganismiStreptococcus pneumoniae
Taxonomic identifieri1313 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2757.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 245245rRNA adenine N-6-methyltransferasePRO_0000101690Add
BLAST

Interactioni

Chemistry

BindingDBiP21236.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni15 – 173Combined sources
Helixi18 – 247Combined sources
Beta strandi29 – 357Combined sources
Helixi45 – 506Combined sources
Beta strandi51 – 6010Combined sources
Beta strandi62 – 687Combined sources
Turni70 – 734Combined sources
Beta strandi75 – 795Combined sources
Turni85 – 884Combined sources
Beta strandi92 – 1009Combined sources
Beta strandi103 – 1053Combined sources
Helixi107 – 11610Combined sources
Beta strandi120 – 12910Combined sources
Helixi130 – 1356Combined sources
Helixi137 – 1393Combined sources
Helixi141 – 1444Combined sources
Turni145 – 1484Combined sources
Beta strandi153 – 1575Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi170 – 1756Combined sources
Helixi184 – 19916Combined sources
Helixi202 – 2054Combined sources
Beta strandi207 – 2093Combined sources
Helixi210 – 2178Combined sources
Helixi229 – 24113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YUBNMR-A1-245[»]
ProteinModelPortaliP21236.
SMRiP21236. Positions 1-245.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21236.

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKNIKYSQN FLTSEKVLNQ IIKQLNLKET DTVYEIGTGK GHLTTKLAKI
60 70 80 90 100
SKQVTSIELD SHLFNLSSEK LKLNIRVTLI HQDILQFQFP NKQRYKIVGS
110 120 130 140 150
IPYHLSTQII KKVVFESHAS DIYLIVEEGF YKRTLDIHRT LGLLLHTQVS
160 170 180 190 200
IQQLLKLPAE CFHPKPKVNS VLIKLTRHTT DVPDKYWKLY TYFVSKWVNR
210 220 230 240
EYRQLFTKNQ FHQAMKHAKV NNLSTITYEQ VLSIFNSYLL FNGRK
Length:245
Mass (Da):28,783
Last modified:May 1, 1991 - v1
Checksum:i5E3AB1BAAA6511C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52632 Genomic DNA. No translation available.
PIRiS12727.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52632 Genomic DNA. No translation available.
PIRiS12727.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YUBNMR-A1-245[»]
ProteinModelPortaliP21236.
SMRiP21236. Positions 1-245.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP21236.
ChEMBLiCHEMBL2757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP21236.

Family and domain databases

Gene3Di1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR001737. KsgA/Erm.
IPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11727. PTHR11727. 1 hit.
PfamiPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTiSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERM_STREE
AccessioniPrimary (citable) accession number: P21236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 11, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Transposable element

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.