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Protein

23S rRNA (guanine(748)-N(1))-methyltransferase

Gene

rlmAII

Organism
Streptomyces fradiae (Streptomyces roseoflavus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Specifically methylates the guanosine in position 748 of 23S rRNA. Confers resistance to the macrolide antibiotic tylosine.3 Publications

Catalytic activityi

S-adenosyl-L-methionine + guanine(748) in 23S rRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(748) in 23S rRNA.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111ZincBy similarity
Metal bindingi14 – 141ZincBy similarity
Metal bindingi27 – 271ZincBy similarity
Metal bindingi31 – 311ZincBy similarity
Binding sitei70 – 701S-adenosyl-L-methionineBy similarity
Binding sitei188 – 1881S-adenosyl-L-methionineBy similarity

GO - Molecular functioni

  • 23S rRNA (guanine(748)-N(1))-methyltransferase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • rRNA base methylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDAi2.1.1.188. 5932.

Names & Taxonomyi

Protein namesi
Recommended name:
23S rRNA (guanine(748)-N(1))-methyltransferase (EC:2.1.1.188)
Alternative name(s):
23S rRNA m1G748 methyltransferase
Tylosin-resistance methyltransferase RlmA(II)
Gene namesi
Name:rlmAII
Synonyms:tlrB
OrganismiStreptomyces fradiae (Streptomyces roseoflavus)
Taxonomic identifieri1906 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 28028023S rRNA (guanine(748)-N(1))-methyltransferasePRO_0000419019Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9S1M6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 1012S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

KOiK14336.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR016718. rRNA_m1G-MeTrfase_A_prd.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PIRSFiPIRSF018249. MyrA_prd. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9S1M6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKNVVRYLR CPHCAAPLRS SDRTLRCENG HTFDVARQGY VNLLRRPTKL
60 70 80 90 100
AADTTDMVAA RAALLDSGHY APLTERLAGT ARRAAGAGAP DCVVDIGGGT
110 120 130 140 150
GHHLARVLEE FEDAEGLLLD MSKPAVRRAA RAHPRASSAV ADVWDTLPLR
160 170 180 190 200
DGAAAMALNV FAPRNPPEIR RILRPGGTLL VVTPQQDHLA ELVDALGLLR
210 220 230 240 250
VRDHKEGRLA EQLAPHFEAV GQERLRTTLR LDHDALGRVV AMGPSSWHQD
260 270 280
PDELARRIAE LPGIHEVTLS VTFTVCRPLP
Length:280
Mass (Da):30,543
Last modified:May 1, 2000 - v1
Checksum:iDC7E039037EBFFFD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821R → G in strain: ATCC 19609.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009971 Genomic DNA. Translation: CAB37345.2.
AF055922 Genomic DNA. Translation: AAD12162.1.
RefSeqiWP_043470786.1. NZ_LGSP01000084.1.

Genome annotation databases

KEGGiag:CAB37345.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009971 Genomic DNA. Translation: CAB37345.2.
AF055922 Genomic DNA. Translation: AAD12162.1.
RefSeqiWP_043470786.1. NZ_LGSP01000084.1.

3D structure databases

ProteinModelPortaliQ9S1M6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAB37345.

Phylogenomic databases

KOiK14336.

Enzyme and pathway databases

BRENDAi2.1.1.188. 5932.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR016718. rRNA_m1G-MeTrfase_A_prd.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PIRSFiPIRSF018249. MyrA_prd. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular analysis of tlrB, an antibiotic-resistance gene from tylosin-producing Streptomyces fradiae, and discovery of a novel resistance mechanism."
    Wilson V.T., Cundliffe E.
    J. Antibiot. 52:288-296(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN ANTIBIOTIC RESISTANCE.
    Strain: C373.1.
  2. "The tylosin biosynthetic cluster from Streptomyces fradiae: genetic organization of the left region."
    Fouces R., Mellado E., Diez B., Barredo J.L.
    Microbiology 145:855-868(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 19609.
  3. "The tylosin resistance gene tlrB of Streptomyces fradiae encodes a methyltransferase that targets G748 in 23S rRNA."
    Liu M., Kirpekar F., Van Wezel G.P., Douthwaite S.
    Mol. Microbiol. 37:811-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
    Strain: ATCC 19609.
  4. "The tylosin-resistance methyltransferase RlmA(II) (TlrB) modifies the N-1 position of 23S rRNA nucleotide G748."
    Douthwaite S., Crain P.F., Liu M., Poehlsgaard J.
    J. Mol. Biol. 337:1073-1077(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiRLMA2_STRFR
AccessioniPrimary (citable) accession number: Q9S1M6
Secondary accession number(s): Q9ZHQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: May 1, 2000
Last modified: November 11, 2015
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.