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P10484 (T1M1_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type I restriction enzyme EcoR124II M protein

Short name=M.EcoR124II
EC=2.1.1.72
Gene names
Name:hsdM
Synonyms:hsm
Encoded onPlasmid IncFIV R124/3
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Methylation of specific adenine residues; required for both restriction and modification activities By similarity. The EcoR124/3 I enzyme recognizes 5'-GAAN7RTCG-3'.

Catalytic activity

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

Subunit structure

The type I restriction/modification system is composed of three polypeptides R, M and S.

Miscellaneous

Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg2+ as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Type I restriction enzyme EcoR124II M protein
PRO_0000088023

Regions

Region198 – 2036S-adenosyl-L-methionine binding By similarity
Region230 – 2323S-adenosyl-L-methionine binding By similarity

Sites

Binding site2541S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
P10484 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 8D82E715F41D94C3

FASTA52058,013
        10         20         30         40         50         60 
MKMTSIQQRA ELHRQIWQIA NDVRGSVDGW DFKQYVLGAL FYRFISENFS SYIEAGDDSI 

        70         80         90        100        110        120 
CYAKLDDSVI TDDIKDDAIK TKGYFIYPSQ LFCNVAAKAN TNDRLNADLN SIFVAIESSA 

       130        140        150        160        170        180 
YGYPSEADIK GLFADFDTTS NRLGNTVKDK NARLAAVLKG VEGLKLGDFN EHQIDLFGDA 

       190        200        210        220        230        240 
YEFLISNYAA NAGKSGGEFF TPQHVSKLIA QLAMHGQTHV NKIYDPAAGS GSLLLQAKKQ 

       250        260        270        280        290        300 
FDNHIIEEGF FGQEINHTTY NLARMNMFLH NINYDKFDIK LGNTLTEPHF RDEKPFDAIV 

       310        320        330        340        350        360 
SNPPYSVKWI GSDDPTLIND ERFAPAGVLA PKSKADFAFV LHALNYLSAK GRAAIVCFPG 

       370        380        390        400        410        420 
IFYRGGAEQK IRQYLVDNNY VETVISLAPN LFFGTTIAVN ILVLSKHKTD TNVQFIDASE 

       430        440        450        460        470        480 
LFKKETNNNI LTDAHIEQIM QVFASKEDVA HLAKSVAFET VVANDYNLSV SSYVEAKDNR 

       490        500        510        520 
EIIDIAELNA ELKTTVSKID QLRKDIDAIV AEIEGCEVQK 

« Hide

References

[1]"Basis for changes in DNA recognition by the EcoR124 and EcoR124/3 type I DNA restriction and modification enzymes."
Price C., Lingner J., Bickle J., Firman T.A., Glover S.W.
J. Mol. Biol. 205:115-125(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13145 Genomic DNA. Translation: CAA31541.1.
PIRS02166.

3D structure databases

ProteinModelPortalP10484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-17004N.

Protein family/group databases

REBASE3392. M.EcoR124I.

Proteomic databases

PRIDEP10484.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.1.1.72. 2026.

Family and domain databases

InterProIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR004546. Restrct_endonuc_typeI_HsdM.
[Graphical view]
PfamPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSPR00507. N12N6MTFRASE.
TIGRFAMsTIGR00497. hsdM. 1 hit.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameT1M1_ECOLX
AccessionPrimary (citable) accession number: P10484
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 16, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries