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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei165 – 1651S-adenosyl-L-methionineCombined sources
Binding sitei195 – 1951S-adenosyl-L-methionine; via carbonyl oxygenCombined sources

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351E → A: Loss of activity. 1 Publication
Mutagenesisi36 – 361D → A: Significantly decreases activity. 1 Publication
Mutagenesisi88 – 881F → A: Significantly decreases activity. 1 Publication
Mutagenesisi91 – 911E → A: Significantly decreases activity. 1 Publication
Mutagenesisi92 – 921R → A: Loss of activity. 1 Publication
Mutagenesisi135 – 1351R → A: Loss of activity. 1 Publication
Mutagenesisi165 – 1651R → A: Significantly decreases activity. 1 Publication
Mutagenesisi219 – 2191S → A: Slightly decreases activity. 1 Publication
Mutagenesisi220 – 2201E → Q: Significantly decreases activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27427423S rRNA (adenosine(1067)-2'-O)-methyltransferasePRO_0000096811Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 239Combined sources
Turni26 – 283Combined sources
Beta strandi31 – 366Combined sources
Helixi37 – 459Combined sources
Beta strandi50 – 567Combined sources
Helixi63 – 719Combined sources
Beta strandi76 – 794Combined sources
Helixi81 – 844Combined sources
Beta strandi96 – 1016Combined sources
Helixi108 – 1147Combined sources
Beta strandi118 – 1236Combined sources
Helixi127 – 13913Combined sources
Beta strandi143 – 1497Combined sources
Helixi158 – 1636Combined sources
Turni164 – 1663Combined sources
Turni168 – 1703Combined sources
Beta strandi173 – 1753Combined sources
Helixi178 – 18710Combined sources
Beta strandi192 – 1954Combined sources
Beta strandi200 – 2023Combined sources
Helixi203 – 2086Combined sources
Beta strandi214 – 2196Combined sources
Turni220 – 2223Combined sources
Helixi226 – 2316Combined sources
Beta strandi235 – 2373Combined sources
Helixi249 – 25911Combined sources
Helixi261 – 27212Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP52391.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 2203S-adenosyl-L-methionine bindingCombined sources
Regioni238 – 2403S-adenosyl-L-methionine bindingCombined sources
Regioni247 – 2526S-adenosyl-L-methionine bindingCombined sources

Sequence similaritiesi

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.

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.

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAB17875.

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: April 13, 2016
This is version 56 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.