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P40813

- T1M_SALTY

UniProt

P40813 - T1M_SALTY

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Protein

Type I restriction enzyme StySJI M protein

Gene

hsdM

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - 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 StySJI enzyme recognizes 5'-GAGN6GTRC-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 sitei216 – 2161S-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

BioCyciSENT99287:GCTI-4557-MONOMER.

Protein family/group databases

REBASEi5596. M.StyLT2ORF4525P.

Names & Taxonomyi

Protein namesi
Recommended name:
Type I restriction enzyme StySJI M protein (EC:2.1.1.72)
Short name:
M.StySJI
Gene namesi
Name:hsdM
Synonyms:hsdT
Ordered Locus Names:STM4525
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Type I restriction enzyme StySJI M proteinPRO_0000088026Add
BLAST

Proteomic databases

PaxDbiP40813.
PRIDEiP40813.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi99287.STM4525.

Structurei

3D structure databases

ProteinModelPortaliP40813.
SMRiP40813. Positions 4-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni148 – 1536S-adenosyl-L-methionine bindingBy similarity
Regioni178 – 1803S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0286.
HOGENOMiHOG000295041.
KOiK03427.
OMAiCDVLRDD.
OrthoDBiEOG686NCV.
PhylomeDBiP40813.

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.

P40813-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNNDLVAKL WKLCDNLRDG GVSYQNYVNE LASLLFLKMC KETGQEADYL
60 70 80 90 100
PEGYRWDDLK SRIGQDQMQF YRNLLVQLGS DEKKLVQAVF HNVSTTIEQP
110 120 130 140 150
KQLTELVSYM DALDWYNGNH GKSRDDFGDM YEGLLQKNAN ETKSGAGQYF
160 170 180 190 200
TPRPLIKTII HLLKPQPREV VQDPAAGTAG FLIEADRYVK SQTNDLDDLD
210 220 230 240 250
GDTQDFQIHR AFIGLELVPG TRRLALMNCL LHDIEGNLDH GGAIRLGNTL
260 270 280 290 300
GSDGENLPKA HIVATNPPFG SAAGTNITRT FVHPTSNKQL CFMQHIIETL
310 320 330 340 350
HPGGRAAVVV PDNVLFEGGK GTDIRRDLMD KCHLHTILRL PTGIFYAQGV
360 370 380 390 400
KTNVLFFTKG TVTNPHQDKN CTDDVWVYDL RTNMPSFGKR TPFTEQHLQP
410 420 430 440 450
FETVYGEDPH GLSPREEGEW SFNAEESEVA DSEENKNTDQ HQATSRWRKF
460 470 480 490 500
SREWIRSAKS DSLDISWLKD KDSIDADSLP EPDVLAAEAM GELVQALGEL
510 520
DALMRELGAG DEADAQRQLL NEAFGEVKA
Length:529
Mass (Da):59,311
Last modified:February 1, 1995 - v1
Checksum:iD5EF542069B8A88A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02506 Unassigned DNA. Translation: AAA19429.1.
AE006468 Genomic DNA. Translation: AAL23343.1.
RefSeqiNP_463384.1. NC_003197.1.
WP_001063190.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL23343; AAL23343; STM4525.
GeneIDi1256051.
KEGGistm:STM4525.
PATRICi32388011. VBISalEnt20916_4768.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02506 Unassigned DNA. Translation: AAA19429.1 .
AE006468 Genomic DNA. Translation: AAL23343.1 .
RefSeqi NP_463384.1. NC_003197.1.
WP_001063190.1. NC_003197.1.

3D structure databases

ProteinModelPortali P40813.
SMRi P40813. Positions 4-525.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 99287.STM4525.

Protein family/group databases

REBASEi 5596. M.StyLT2ORF4525P.

Proteomic databases

PaxDbi P40813.
PRIDEi P40813.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL23343 ; AAL23343 ; STM4525 .
GeneIDi 1256051.
KEGGi stm:STM4525.
PATRICi 32388011. VBISalEnt20916_4768.

Phylogenomic databases

eggNOGi COG0286.
HOGENOMi HOG000295041.
KOi K03427.
OMAi CDVLRDD.
OrthoDBi EOG686NCV.
PhylomeDBi P40813.

Enzyme and pathway databases

BioCyci SENT99287:GCTI-4557-MONOMER.

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

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.

Entry informationi

Entry nameiT1M_SALTY
AccessioniPrimary (citable) accession number: P40813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 1, 2014
This is version 96 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

Complete proteome, Reference proteome

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