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Protein

23S rRNA (adenosine(1067)-2'-O)-methyltransferase

Gene

nshR

Organism
Streptomyces actuosus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Specifically methylates the adenosine-1067 in 23S ribosomal RNA. Confers resistance to antibiotic nosiheptide.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + adenosine(1067) in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyladenosine(1067) in 23S rRNA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei165S-adenosyl-L-methionineCombined sources1
Binding sitei195S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.230. 12393.

Names & Taxonomyi

Protein namesi
Recommended name:
23S rRNA (adenosine(1067)-2'-O)-methyltransferaseCurated (EC:2.1.1.2301 Publication)
Alternative name(s):
Nosiheptide-resistance methyltransferase2 Publications
Short name:
NHR1 Publication
Short name:
NSR1 Publication
Gene namesi
Name:nshRImported
OrganismiStreptomyces actuosus
Taxonomic identifieri1885 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi35E → A: Loss of activity. 1 Publication1
Mutagenesisi36D → A: Significantly decreases activity. 1 Publication1
Mutagenesisi88F → A: Significantly decreases activity. 1 Publication1
Mutagenesisi91E → A: Significantly decreases activity. 1 Publication1
Mutagenesisi92R → A: Loss of activity. 1 Publication1
Mutagenesisi135R → A: Loss of activity. 1 Publication1
Mutagenesisi165R → A: Significantly decreases activity. 1 Publication1
Mutagenesisi219S → A: Slightly decreases activity. 1 Publication1
Mutagenesisi220E → Q: Significantly decreases activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000968111 – 27423S rRNA (adenosine(1067)-2'-O)-methyltransferaseAdd BLAST274

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 23Combined sources9
Turni26 – 28Combined sources3
Beta strandi31 – 36Combined sources6
Helixi37 – 45Combined sources9
Beta strandi50 – 56Combined sources7
Helixi63 – 71Combined sources9
Beta strandi76 – 79Combined sources4
Helixi81 – 84Combined sources4
Beta strandi96 – 101Combined sources6
Helixi108 – 114Combined sources7
Beta strandi118 – 123Combined sources6
Helixi127 – 139Combined sources13
Beta strandi143 – 149Combined sources7
Helixi158 – 163Combined sources6
Turni164 – 166Combined sources3
Turni168 – 170Combined sources3
Beta strandi173 – 175Combined sources3
Helixi178 – 187Combined sources10
Beta strandi192 – 195Combined sources4
Beta strandi200 – 202Combined sources3
Helixi203 – 208Combined sources6
Beta strandi214 – 219Combined sources6
Turni220 – 222Combined sources3
Helixi226 – 231Combined sources6
Beta strandi235 – 237Combined sources3
Helixi249 – 259Combined sources11
Helixi261 – 272Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NK6X-ray2.00A/B1-274[»]
3NK7X-ray2.10A/B1-274[»]
ProteinModelPortaliP52391.
SMRiP52391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52391.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni218 – 220S-adenosyl-L-methionine bindingCombined sources3
Regioni238 – 240S-adenosyl-L-methionine bindingCombined sources3
Regioni247 – 252S-adenosyl-L-methionine bindingCombined sources6

Sequence similaritiesi

Phylogenomic databases

KOiK05926.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
3.40.1280.10. 1 hit.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR029064. L30e-like.
IPR001537. SpoU_MeTrfase.
IPR006795. Thiostrepton-R_Mease_TSNR_N.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PfamiPF00588. SpoU_methylase. 1 hit.
PF04705. TSNR_N. 1 hit.
[Graphical view]
ProDomiPD407686. Thiostrepton-R_Mease_TSNR_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF75217. SSF75217. 1 hit.

Sequencei

Sequence statusi: Complete.

P52391-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEPAIITNA SDPAVQRIID VTKHSRASIK TTLIEDTEPL MECIRAGVQF
60 70 80 90 100
IEVYGSSGTP LDPALLDLCR QREIPVRLID VSIVNQLFKA ERKAKVFGIA
110 120 130 140 150
RVPRPARLAD IAERGGDVVV LDGVKIVGNI GAIVRTSLAL GAAGIVLVDS
160 170 180 190 200
DLATIADRRL LRASRGYVFS LPVVLADREE AVSFLRDNDI ALMVLDTDGD
210 220 230 240 250
LGVKDLGDRA DRMALVFGSE KGGPSGLFQE ASAGTVSIPM LSSTESLNVS
260 270
VSVGIALHER SARNFAVRRA AAQA
Length:274
Mass (Da):29,184
Last modified:October 1, 1996 - v1
Checksum:i9FA2C12B2E8BF24D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75434 Genomic DNA. Translation: AAB17875.1.
PIRiJQ0686.
RefSeqiWP_063854493.1. NG_048019.1.

Genome annotation databases

KEGGiag:AAB17875.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75434 Genomic DNA. Translation: AAB17875.1.
PIRiJQ0686.
RefSeqiWP_063854493.1. NG_048019.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NK6X-ray2.00A/B1-274[»]
3NK7X-ray2.10A/B1-274[»]
ProteinModelPortaliP52391.
SMRiP52391.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAB17875.

Phylogenomic databases

KOiK05926.

Enzyme and pathway databases

BRENDAi2.1.1.230. 12393.

Miscellaneous databases

EvolutionaryTraceiP52391.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
3.40.1280.10. 1 hit.
InterProiIPR029028. Alpha/beta_knot_MTases.
IPR029064. L30e-like.
IPR001537. SpoU_MeTrfase.
IPR006795. Thiostrepton-R_Mease_TSNR_N.
IPR029026. tRNA_m1G_MTases_N.
[Graphical view]
PfamiPF00588. SpoU_methylase. 1 hit.
PF04705. TSNR_N. 1 hit.
[Graphical view]
ProDomiPD407686. Thiostrepton-R_Mease_TSNR_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF75217. SSF75217. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNSHR_STRAS
AccessioniPrimary (citable) accession number: P52391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 59 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

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.