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Protein

Type I restriction enzyme EcoEI M protein

Gene

hsdM

Organism
Escherichia coli
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

The M and S subunits together form a methyltransferase (MTase) that methylates two adenine residues in complementary strands of a bipartite DNA recognition sequence. In the presence of the R subunit the complex can also act as an endonuclease, binding to the same target sequence but cutting the DNA some distance from this site. Whether the DNA is cut or modified depends on the methylation state of the target sequence. When the target site is unmodified, the DNA is cut. When the target site is hemimethylated, the complex acts as a maintenance MTase modifying the DNA so that both strands become methylated. The EcoEI enzyme recognizes 5'-GAGN7ATGC-3'.

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.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei226S-adenosyl-L-methionineBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processRestriction system
LigandS-adenosyl-L-methionine

Protein family/group databases

REBASEi101119 M.Rga602ORF2367P

Names & Taxonomyi

Protein namesi
Recommended name:
Type I restriction enzyme EcoEI M protein (EC:2.1.1.72)
Short name:
M.EcoEI
Gene namesi
Name:hsdM
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000880211 – 490Type I restriction enzyme EcoEI M proteinAdd BLAST490

Proteomic databases

PRIDEiQ47282

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ47282
SMRiQ47282
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni163 – 168S-adenosyl-L-methionine bindingBy similarity6
Regioni193 – 195S-adenosyl-L-methionine bindingBy similarity3

Sequence similaritiesi

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

Family and domain databases

Gene3Di1.20.1260.30, 1 hit
InterProiView protein in InterPro
IPR022749 D12N6_MeTrfase_N
IPR038333 D12N6_MeTrfase_N_sf
IPR003356 DNA_methylase_A-5
IPR002052 DNA_methylase_N6_adenine_CS
IPR029063 SAM-dependent_MTases
PfamiView protein in Pfam
PF12161 HsdM_N, 1 hit
PF02384 N6_Mtase, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS00092 N6_MTASE, 1 hit

Sequencei

Sequence statusi: Complete.

Q47282-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSISSVIKSL QDIMRKDAGV DGDAQRLGQL SWLLFLKIFD TQEEELELEQ
60 70 80 90 100
DDYQFPIPQR YLWRSWAANS EGITGDALLE FVNDDLFPTL KNLTAPIDKN
110 120 130 140 150
PRGFVVKQAF SDAYNYMKNG TLLRQVINKL NEIDFSSSQE RHLFGDIYEQ
160 170 180 190 200
ILRDLQSAGN AGEFYTPRAV TRFMVNRIDP KLGESIMDPA CGTGGFLACA
210 220 230 240 250
FDHVKDNYVK TTEDHKTLQQ QIYGVEKKQL PHLLCTTNML LHGIEVPVQI
260 270 280 290 300
RHDNTLNKPL SSWDEQVDVI VTNPPFGGTE EDGIEKNFPA EMQTRETADL
310 320 330 340 350
FLQLIIEVLA DKGRAAVVLP DGTLFGEGVK TKIKKLLTEE CNLHTIVRLP
360 370 380 390 400
NGVFNPYTGI KTNILFFTKG QPTKEVWFYE HPYPDGVKNY SKTKPMKFEE
410 420 430 440 450
FQAEIDWWGN EADDFASREE NNQAWKVGID DIIARNFNLD IKNPYQGETI
460 470 480 490
SHDPDELLAQ YQTQQAEIGE LRNQLRDILG AALAGNKGAN
Length:490
Mass (Da):55,620
Last modified:November 1, 1996 - v1
Checksum:iA8643DEB39981FFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18759 Genomic DNA Translation: AAD15049.1
PIRiI41293
RefSeqiWP_058649287.1, NZ_NMFU01000051.1

Similar proteinsi

Entry informationi

Entry nameiT1ME_ECOLX
AccessioniPrimary (citable) accession number: Q47282
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 81 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health