P14751 (MTR1_RHOSH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Modification methylase RsrI
Short name=M.RsrI
EC=2.1.1.72

Alternative name(s):
Adenine-specific methyltransferase RsrI

Gene names

Name:

rsrIM

Organism

Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)

Taxonomic identifier

1063 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.
Sequence similarities	Belongs to the N(4)/N(6)-methyltransferase family.

Ontologies

Keywords
Biological process	Restriction system
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	DNA methylation on adenine Inferred from electronic annotation. Source: GOC DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro N-methyltransferase activity Inferred from electronic annotation. Source: InterPro site-specific DNA-methyltransferase (adenine-specific) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 319

319

Modification methylase RsrI

PRO_0000087970

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

319

Helix Strand Turn

Details...

Beta strand

38 – 44

7

Helix

47 – 52

6

Beta strand

59 – 64

6

Helix

72 – 76

5

Helix

81 – 95

15

Beta strand

96 – 106

11

Helix

119 – 129

11

Beta strand

133 – 141

9

Beta strand

149 – 151

3

Beta strand

156 – 165

10

Helix

173 – 175

3

Helix

181 – 188

8

Helix

195 – 200

6

Beta strand

206 – 209

4

Helix

229 – 239

11

Beta strand

245 – 248

4

Turn

252 – 254

3

Helix

255 – 263

9

Beta strand

266 – 273

8

Helix

275 – 286

12

Beta strand

299 – 303

5

Helix

305 – 308

4

Helix

309 – 312

4

Sequences

	Sequence		Length	Mass (Da)
	P14751 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 806E7BF702D4EC85	FASTA	319	35,655
	10 20 30 40 50 60 MANRSHHNAG HRAMNALRKS GQKHSSESQL GSSEIGTTRH VYDVCDCLDT LAKLPDDSVQ 70 80 90 100 110 120 LIICDPPYNI MLADWDDHMD YIGWAKRWLA EAERVLSPTG SIAIFGGLQY QGEAGSGDLI 130 140 150 160 170 180 SIISHMRQNS KMLLANLIIW NYPNGMSAQR FFANRHEEIA WFAKTKKYFF DLDAVREPYD 190 200 210 220 230 240 EETKAAYMKD KRLNPESVEK GRNPTNVWRM SRLNGNSLER VGHPTQKPAA VIERLVRALS 250 260 270 280 290 300 HPGSTVLDFF AGSGVTARVA IQEGRNSICT DAAPVFKEYY QKQLTFLQDD GLIDKARSYE 310 IVEGAANFGA ALQRGDVAS

References

[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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16456 Genomic DNA. Translation: CAA34475.1.

PIR

S07570.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P14751.

SMR

P14751. Positions 36-314.

ModBase

Search...

Protein family/group databases

REBASE

3487. M.RsrI.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002295. D21N6_MeTrfase.
IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
[Graphical view]

Pfam

PF01555. N6_N4_Mtase. 1 hit.
[Graphical view]

PRINTS

PR00506. D21N6MTFRASE.

PROSITE

PS00092. N6_MTASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P14751.

Entry information

Entry name

MTR1_RHOSH

Accession

Primary (citable) accession number: P14751

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	April 3, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program