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Protein

Type I restriction enzyme EcoR124II M protein

Gene

hsdM

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

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-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

Enzyme and pathway databases

BRENDAi2.1.1.72. 2026.

Protein family/group databases

REBASEi3392. M.EcoR124I.

Names & Taxonomyi

Protein namesi
Recommended name:
Type I restriction enzyme EcoR124II M protein (EC:2.1.1.72)
Short name:
M.EcoR124II
Gene namesi
Name:hsdM
Synonyms:hsm
Encoded oniPlasmid IncFIV R124/30 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Type I restriction enzyme EcoR124II M proteinPRO_0000088023Add
BLAST

Proteomic databases

PRIDEiP10484.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-17004N.

Structurei

3D structure databases

ProteinModelPortaliP10484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

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

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.
[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.

P10484-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKMTSIQQRA ELHRQIWQIA NDVRGSVDGW DFKQYVLGAL FYRFISENFS
60 70 80 90 100
SYIEAGDDSI CYAKLDDSVI TDDIKDDAIK TKGYFIYPSQ LFCNVAAKAN
110 120 130 140 150
TNDRLNADLN SIFVAIESSA YGYPSEADIK GLFADFDTTS NRLGNTVKDK
160 170 180 190 200
NARLAAVLKG VEGLKLGDFN EHQIDLFGDA YEFLISNYAA NAGKSGGEFF
210 220 230 240 250
TPQHVSKLIA QLAMHGQTHV NKIYDPAAGS GSLLLQAKKQ FDNHIIEEGF
260 270 280 290 300
FGQEINHTTY NLARMNMFLH NINYDKFDIK LGNTLTEPHF RDEKPFDAIV
310 320 330 340 350
SNPPYSVKWI GSDDPTLIND ERFAPAGVLA PKSKADFAFV LHALNYLSAK
360 370 380 390 400
GRAAIVCFPG IFYRGGAEQK IRQYLVDNNY VETVISLAPN LFFGTTIAVN
410 420 430 440 450
ILVLSKHKTD TNVQFIDASE LFKKETNNNI LTDAHIEQIM QVFASKEDVA
460 470 480 490 500
HLAKSVAFET VVANDYNLSV SSYVEAKDNR EIIDIAELNA ELKTTVSKID
510 520
QLRKDIDAIV AEIEGCEVQK
Length:520
Mass (Da):58,013
Last modified:July 1, 1989 - v1
Checksum:i8D82E715F41D94C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13145 Genomic DNA. Translation: CAA31541.1.
PIRiS02166.
RefSeqiWP_032491648.1. NG_036184.1.
YP_009080452.1. NG_036184.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13145 Genomic DNA. Translation: CAA31541.1.
PIRiS02166.
RefSeqiWP_032491648.1. NG_036184.1.
YP_009080452.1. NG_036184.1.

3D structure databases

ProteinModelPortaliP10484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-17004N.

Protein family/group databases

REBASEi3392. M.EcoR124I.

Proteomic databases

PRIDEiP10484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.1.1.72. 2026.

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.
[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]
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiT1M1_ECOLX
AccessioniPrimary (citable) accession number: P10484
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 7, 2015
This is version 94 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.

Keywords - Technical termi

Plasmid

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.