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Q47163

- T1MP_ECOLX

UniProt

Q47163 - T1MP_ECOLX

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Protein
Type I restriction enzyme EcoprrI 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 EcoprrI enzyme recognizes 5'-CCAN7ATGC-3'.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei254 – 2541S-adenosyl-L-methionine By 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
Complete GO annotation...

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

REBASEi3552. M.EcoprrI.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Type I restriction enzyme EcoprrI M protein
PRO_0000088024Add
BLAST

Proteomic databases

PRIDEiQ47163.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ47163.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2036S-adenosyl-L-methionine binding By similarity
Regioni230 – 2323S-adenosyl-L-methionine binding By similarity

Sequence similaritiesi

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.
IPR004546. Restrct_endonuc_typeI_HsdM.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00507. N12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 2 hits.
TIGRFAMsiTIGR00497. hsdM. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q47163-1 [UniParc]FASTAAdd to Basket

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MKMTSIQQRA ELHRQIWQIA NDVRGSVDGW DFKQYVLGAL FYRFISENFS    50
SYIEAGDDSI CYAKLDDSVI TDDIKDDAIK TKGYFIYPSQ LFCNVAAKAN 100
TNDRLNADLN SIFVAIESSA YGYPSEADIK GLFADFDTTS NRLGNTVKDK 150
NARLAAVLKG VEGLKLGDFN EHQIDLFGDA YEFLISNYAA NAGKSGGEFF 200
TPQHVSKLIA QLAMHGQTHV NKIYDPAAGS GSLLLQAKKQ FDDHIIEEGF 250
FGQEINHTTY NLARMNMFLH NINYDKFDIK LGNTLTEPHF RDEKPFDAIV 300
SNPPYSVKWI GSDDPTLIND ERFAPAGVLA PKSKADFAFV LHALNYLSAK 350
GRAAIVCFPG IFYRGGAEQK IRQYLVDNNY VETVISLAPN LFFGTTIAVN 400
ILVLSKHKTD TKVQFIDASE LFKKETNNNI LTDAHIEQIM QVFASKEDVA 450
HLAKSVAFET VVANDYNLSV SSYVEAKDTR EIIDIAELNA ELKTTVSKID 500
QLRKDIDAIV AEIEGCEVQK 520
Length:520
Mass (Da):58,015
Last modified:November 1, 1996 - v1
Checksum:i79401EC1720EB257
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75452 Genomic DNA. Translation: CAA53205.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75452 Genomic DNA. Translation: CAA53205.1 .

3D structure databases

ProteinModelPortali Q47163.
ModBasei Search...

Protein family/group databases

REBASEi 3552. M.EcoprrI.

Proteomic databases

PRIDEi Q47163.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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.
IPR004546. Restrct_endonuc_typeI_HsdM.
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. 2 hits.
TIGRFAMsi TIGR00497. hsdM. 1 hit.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The Escherichia coli prr region encodes a functional type IC DNA restriction system closely integrated with an anticodon nuclease gene."
    Tyndall C., Meister J., Bickle T.A.
    J. Mol. Biol. 237:266-274(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CTR5X.

Entry informationi

Entry nameiT1MP_ECOLX
AccessioniPrimary (citable) accession number: Q47163
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 1, 1996
Last modified: June 11, 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

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