Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P40813 (T1M_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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 StySJI M protein

Short name=M.StySJI
EC=2.1.1.72
Gene names
Name:hsdM
Synonyms:hsdT
Ordered Locus Names:STM4525
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [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. The StySJI enzyme recognizes 5'-GAGN6GTRC-3'.

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 StySJI M protein
PRO_0000088026

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
P40813 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: D5EF542069B8A88A

FASTA52959,311
        10         20         30         40         50         60 
MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEADYL PEGYRWDDLK 

        70         80         90        100        110        120 
SRIGQDQMQF YRNLLVQLGS DEKKLVQAVF HNVSTTIEQP KQLTELVSYM DALDWYNGNH 

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

       190        200        210        220        230        240 
FLIEADRYVK SQTNDLDDLD GDTQDFQIHR AFIGLELVPG TRRLALMNCL LHDIEGNLDH 

       250        260        270        280        290        300 
GGAIRLGNTL GSDGENLPKA HIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL 

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

       370        380        390        400        410        420 
TVTNPHQDKN CTDDVWVYDL RTNMPSFGKR TPFTEQHLQP FETVYGEDPH GLSPREEGEW 

       430        440        450        460        470        480 
SFNAEESEVA DSEENKNTDQ HQATSRWRKF SREWIRSAKS DSLDISWLKD KDSIDADSLP 

       490        500        510        520 
EPDVLAAEAM GELVQALGEL DALMRELGAG DEADAQRQLL NEAFGEVKA 

« Hide

References

« Hide 'large scale' 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].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02506 Unassigned DNA. Translation: AAA19429.1.
AE006468 Genomic DNA. Translation: AAL23343.1.
RefSeqNP_463384.1. NC_003197.1.

3D structure databases

ProteinModelPortalP40813.
SMRP40813. Positions 4-525.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM4525.

Protein family/group databases

REBASE5596. M.StyLT2ORF4525P.

Proteomic databases

PaxDbP40813.
PRIDEP40813.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL23343; AAL23343; STM4525.
GeneID1256051.
KEGGstm:STM4525.
PATRIC32388011. VBISalEnt20916_4768.

Phylogenomic databases

eggNOGCOG0286.
HOGENOMHOG000295041.
KOK03427.
OMACDVLRDD.
OrthoDBEOG686NCV.
PhylomeDBP40813.

Enzyme and pathway databases

BioCycSENT99287:GCTI-4557-MONOMER.

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_SALTY
AccessionPrimary (citable) accession number: P40813
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 94 of the entry and version 1 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