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Q47282

- T1ME_ECOLX

UniProt

Q47282 - T1ME_ECOLX

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Protein

Type I restriction enzyme EcoEI M protein

Gene

hsdM

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- 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'.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei226 – 2261S-adenosyl-L-methionineBy similarity

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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Type I restriction enzyme EcoEI M proteinPRO_0000088021Add
BLAST

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni163 – 1686S-adenosyl-L-methionine bindingBy similarity
Regioni193 – 1953S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0286.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00507. N12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18759 Genomic DNA. Translation: AAD15049.1 .
PIRi I41293.

3D structure databases

ProteinModelPortali Q47282.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q47282.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0286.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view ]
PRINTSi PR00507. N12N6MTFRASE.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymes."
    Murray N.E., Daniel A.S., Cowan G.M., Sharp P.M.
    Mol. Microbiol. 9:133-143(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A58.

Entry informationi

Entry nameiT1ME_ECOLX
AccessioniPrimary (citable) accession number: Q47282
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: October 1, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Documents

  1. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3