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P07989 (T1M_SALPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 68. 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 StySPI M protein

Short name=M.StySPI
EC=2.1.1.72
Gene names
Name:hsdM
Synonyms:hsdT
OrganismSalmonella potsdam
Taxonomic identifier597 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length529 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.

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 – 529529Type I restriction enzyme StySPI M protein
PRO_0000088025

Regions

Region148 – 1536S-adenosyl-L-methionine binding By similarity
Region178 – 1803S-adenosyl-L-methionine binding By similarity

Sites

Binding site2161S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
P07989 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 07895A9ADA4FA249

FASTA52958,906
        10         20         30         40         50         60 
MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEADYL PEGYRWDDLK 

        70         80         90        100        110        120 
SRIGQEQLQF YRNLLVHLGA DEKKLVQAVF QNVNTTITQP KQLTELVSSM DSLDWYNGDH 

       130        140        150        160        170        180 
GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF TPRPLIKTII HLLKPQPREV VQDPAAGTAG 

       190        200        210        220        230        240 
FLIEADRYVK SQTNDLDDLD GDAQDFQIKK AFVGLELVPG TRRLALMNCL LHDIEGNLDH 

       250        260        270        280        290        300 
GGAIRLGNTL GSDGENLPQA DIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL 

       310        320        330        340        350        360 
PPGGRAAAVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV KTNVLFFTKG 

       370        380        390        400        410        420 
TVANPNQDKN CTDDVWVYDL RTNMPSFGKR TPFTEQHLQP FETVYGEDPH GLSPRTEGEW 

       430        440        450        460        470        480 
SFNAEESEVA DSEENKNADQ HQATSRWRKF SREWIRTAKS DSLDISWLKD KDSIDADSLP 

       490        500        510        520 
EPDVLAAEAM GELVQALGEL DALMRELGAG DEADAQRQLL EEAFGGVKA 

« Hide

References

[1]"Roles of selection and recombination in the evolution of type I restriction-modification systems in enterobacteria."
Sharp P.M., Kelleher J.E., Daniel A.S., Cowan G.M., Murray N.E.
Proc. Natl. Acad. Sci. U.S.A. 89:9836-9840(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Two DNA recognition domains of the specificity polypeptides of a family of type I restriction enzymes."
Fuller-Pace F.V., Murray N.E.
Proc. Natl. Acad. Sci. U.S.A. 83:9368-9372(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 455-529.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02507 Genomic DNA. Translation: AAA27143.1.
M14984 Genomic DNA. Translation: AAA27144.1.

3D structure databases

ProteinModelPortalP07989.
SMRP07989. Positions 4-527.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

REBASE3518. M.StySPI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSPR00507. N12N6MTFRASE.
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameT1M_SALPO
AccessionPrimary (citable) accession number: P07989
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 68 of the entry and version 2 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