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Protein

Modification methylase RsrI

Gene

rsrIM

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

This methylase recognizes the double-stranded sequence GAATTC, causes specific methylation on A-? on both strands, and protects the DNA from cleavage by the RsrI endonuclease.

Catalytic activityi

S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.72. 5383.

Protein family/group databases

REBASEi3487. M.RsrI.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase RsrI (EC:2.1.1.72)
Short name:
M.RsrI
Alternative name(s):
Adenine-specific methyltransferase RsrI
Gene namesi
Name:rsrIM
OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifieri1063 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000879701 – 319Modification methylase RsrIAdd BLAST319

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 44Combined sources7
Helixi47 – 52Combined sources6
Beta strandi59 – 64Combined sources6
Helixi72 – 76Combined sources5
Helixi81 – 95Combined sources15
Beta strandi96 – 106Combined sources11
Helixi119 – 129Combined sources11
Beta strandi133 – 141Combined sources9
Beta strandi149 – 151Combined sources3
Beta strandi156 – 165Combined sources10
Helixi173 – 175Combined sources3
Helixi181 – 188Combined sources8
Helixi195 – 200Combined sources6
Beta strandi206 – 209Combined sources4
Helixi229 – 239Combined sources11
Beta strandi245 – 248Combined sources4
Turni252 – 254Combined sources3
Helixi255 – 263Combined sources9
Beta strandi266 – 273Combined sources8
Helixi275 – 286Combined sources12
Beta strandi299 – 303Combined sources5
Helixi305 – 308Combined sources4
Helixi309 – 312Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG2X-ray1.75A1-319[»]
1NW5X-ray2.05A1-319[»]
1NW6X-ray1.94A1-319[»]
1NW7X-ray2.10A1-319[»]
1NW8X-ray2.25A1-319[»]
ProteinModelPortaliP14751.
SMRiP14751.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14751.

Family & Domainsi

Sequence similaritiesi

Belongs to the N(4)/N(6)-methyltransferase family.Curated

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR002295. D21N6_MeTrfase.
IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00506. D21N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14751-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANRSHHNAG HRAMNALRKS GQKHSSESQL GSSEIGTTRH VYDVCDCLDT
60 70 80 90 100
LAKLPDDSVQ LIICDPPYNI MLADWDDHMD YIGWAKRWLA EAERVLSPTG
110 120 130 140 150
SIAIFGGLQY QGEAGSGDLI SIISHMRQNS KMLLANLIIW NYPNGMSAQR
160 170 180 190 200
FFANRHEEIA WFAKTKKYFF DLDAVREPYD EETKAAYMKD KRLNPESVEK
210 220 230 240 250
GRNPTNVWRM SRLNGNSLER VGHPTQKPAA VIERLVRALS HPGSTVLDFF
260 270 280 290 300
AGSGVTARVA IQEGRNSICT DAAPVFKEYY QKQLTFLQDD GLIDKARSYE
310
IVEGAANFGA ALQRGDVAS
Length:319
Mass (Da):35,655
Last modified:April 1, 1990 - v1
Checksum:i806E7BF702D4EC85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16456 Genomic DNA. Translation: CAA34475.1.
PIRiS07570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16456 Genomic DNA. Translation: CAA34475.1.
PIRiS07570.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG2X-ray1.75A1-319[»]
1NW5X-ray2.05A1-319[»]
1NW6X-ray1.94A1-319[»]
1NW7X-ray2.10A1-319[»]
1NW8X-ray2.25A1-319[»]
ProteinModelPortaliP14751.
SMRiP14751.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi3487. M.RsrI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.1.1.72. 5383.

Miscellaneous databases

EvolutionaryTraceiP14751.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR002295. D21N6_MeTrfase.
IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00506. D21N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTR1_RHOSH
AccessioniPrimary (citable) accession number: P14751
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: November 2, 2016
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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  3. 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.