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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)DescriptionActionsGraphical viewLength
Binding sitei10S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei12S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1
Binding sitei37S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
Binding sitei58S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei83S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei100S-adenosyl-L-methioninePROSITE-ProRule annotation1

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 databases

ChEMBLiCHEMBL2757.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001016901 – 245rRNA adenine N-6-methyltransferaseAdd BLAST245

Interactioni

Chemistry databases

BindingDBiP21236.

Structurei

Secondary structure

1245
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni15 – 17Combined sources3
Helixi18 – 24Combined sources7
Beta strandi29 – 35Combined sources7
Helixi45 – 50Combined sources6
Beta strandi51 – 60Combined sources10
Beta strandi62 – 68Combined sources7
Turni70 – 73Combined sources4
Beta strandi75 – 79Combined sources5
Turni85 – 88Combined sources4
Beta strandi92 – 100Combined sources9
Beta strandi103 – 105Combined sources3
Helixi107 – 116Combined sources10
Beta strandi120 – 129Combined sources10
Helixi130 – 135Combined sources6
Helixi137 – 139Combined sources3
Helixi141 – 144Combined sources4
Turni145 – 148Combined sources4
Beta strandi153 – 157Combined sources5
Beta strandi162 – 165Combined sources4
Beta strandi170 – 175Combined sources6
Helixi184 – 199Combined sources16
Helixi202 – 205Combined sources4
Beta strandi207 – 209Combined sources3
Helixi210 – 217Combined sources8
Helixi229 – 241Combined sources13

3D structure databases

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

Chemistry databases

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 2, 2016
This is version 94 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.