SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P14751

- MTR1_RHOSH

UniProt

P14751 - MTR1_RHOSH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Modification methylase RsrI

Gene
rsrIM
Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed - Annotation score: 3 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 + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. N-methyltransferase activity Source: InterPro
  3. site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319Modification methylase RsrIPRO_0000087970Add
BLAST

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 447
Helixi47 – 526
Beta strandi59 – 646
Helixi72 – 765
Helixi81 – 9515
Beta strandi96 – 10611
Helixi119 – 12911
Beta strandi133 – 1419
Beta strandi149 – 1513
Beta strandi156 – 16510
Helixi173 – 1753
Helixi181 – 1888
Helixi195 – 2006
Beta strandi206 – 2094
Helixi229 – 23911
Beta strandi245 – 2484
Turni252 – 2543
Helixi255 – 2639
Beta strandi266 – 2738
Helixi275 – 28612
Beta strandi299 – 3035
Helixi305 – 3084
Helixi309 – 3124

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 36-314.

Miscellaneous databases

EvolutionaryTraceiP14751.

Family & Domainsi

Sequence similaritiesi

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-like.
[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

MANRSHHNAG HRAMNALRKS GQKHSSESQL GSSEIGTTRH VYDVCDCLDT    50
LAKLPDDSVQ LIICDPPYNI MLADWDDHMD YIGWAKRWLA EAERVLSPTG 100
SIAIFGGLQY QGEAGSGDLI SIISHMRQNS KMLLANLIIW NYPNGMSAQR 150
FFANRHEEIA WFAKTKKYFF DLDAVREPYD EETKAAYMKD KRLNPESVEK 200
GRNPTNVWRM SRLNGNSLER VGHPTQKPAA VIERLVRALS HPGSTVLDFF 250
AGSGVTARVA IQEGRNSICT DAAPVFKEYY QKQLTFLQDD GLIDKARSYE 300
IVEGAANFGA ALQRGDVAS 319
Length:319
Mass (Da):35,655
Last modified:April 1, 1990 - v1
Checksum:i806E7BF702D4EC85
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16456 Genomic DNA. Translation: CAA34475.1.
PIRiS07570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16456 Genomic DNA. Translation: CAA34475.1 .
PIRi S07570.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EG2 X-ray 1.75 A 1-319 [» ]
1NW5 X-ray 2.05 A 1-319 [» ]
1NW6 X-ray 1.94 A 1-319 [» ]
1NW7 X-ray 2.10 A 1-319 [» ]
1NW8 X-ray 2.25 A 1-319 [» ]
ProteinModelPortali P14751.
SMRi P14751. Positions 36-314.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 3487. M.RsrI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P14751.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR002295. D21N6_MeTrfase.
IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF01555. N6_N4_Mtase. 1 hit.
[Graphical view ]
PRINTSi PR00506. D21N6MTFRASE.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Purification, cloning and sequence analysis of RsrI DNA methyltransferase: lack of homology between two enzymes, RsrI and EcoRI, that methylate the same nucleotide in identical recognition sequences."
    Kaszubska W., Aiken C., O'Connor D., Gumport R.I., Stephenson F.H., Greene P.J.
    Nucleic Acids Res. 17:10403-10425(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 630.
  2. "Nucleotide sequence of the gene encoding the RsrI methyltransferase."
    Stephenson F.H., Greene P.J.
    Nucleic Acids Res. 17:10503-10503(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 630.
  3. "Structure of RsrI methyltransferase, a member of the N6-adenine beta class of DNA methyltransferases."
    Scavetta R.D., Thomas C.B., Walsh M.A., Szegedi S., Joachimiak A., Gumport R.I., Churchill M.E.
    Nucleic Acids Res. 28:3950-3961(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

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: June 11, 2014
This is version 83 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

External Data

Dasty 3