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Protein

Type III restriction-modification system StyLTI enzyme mod

Gene

mod

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Binds the system-specific DNA recognition site 5'-CAGAG-3'. Necessary for restriction and for methylation of A-4.

Catalytic activityi

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  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

DNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciSENT99287:GCTI-358-MONOMER.

Protein family/group databases

REBASEi5598. M.StyLT2ORF357P.

Names & Taxonomyi

Protein namesi
Recommended name:
Type III restriction-modification system StyLTI enzyme mod (EC:2.1.1.72)
Short name:
M.StyLTI
Alternative name(s):
StyLTI methyltransferase
Gene namesi
Name:mod
Ordered Locus Names:STM0357
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 – 652652Type III restriction-modification system StyLTI enzyme modPRO_0000088032Add
BLAST

Proteomic databases

PaxDbiP40814.
PRIDEiP40814.

Interactioni

Subunit structurei

Contains two different subunits: res and mod. Mod is a homotetramer (By similarity).By similarity

Protein-protein interaction databases

STRINGi99287.STM0357.

Structurei

3D structure databases

ProteinModelPortaliP40814.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 1384Binding of S-adenosyl methionineSequence Analysis

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2189.
HOGENOMiHOG000253523.
KOiK07316.
OMAiPYSVFYQ.
OrthoDBiEOG6W9X8K.

Family and domain databases

Gene3Di3.40.50.150. 3 hits.
InterProiIPR002295. D21N6_MeTrfase.
IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PIRSFiPIRSF015855. TypeIII_Mtase_mKpnI. 1 hit.
PRINTSiPR00506. D21N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 3 hits.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40814-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKDNQKHNE SVAPNSAFLS ELQRALPEFF TADRYNEQGE LIAKGGFDLA
60 70 80 90 100
RFERALKARN IDELTSGYQI DFIGKDYAKK QAGEKSVTVI VPDVEHNTLA
110 120 130 140 150
ENKNSHNLFL TGDNLDVLRH LQNNYADTVD MIYIDPPYNT GSDGFVYPDH
160 170 180 190 200
FEYSDRALQD MFGLNDTELA RLKSIQGKST HSAWLSFMYP RLFLARKLLK
210 220 230 240 250
DTGFIFISID DNEYANLKLM MDEIFGEGGF VTNVMWKRKK EISNDSDNVS
260 270 280 290 300
IQGEYILVYA KTGQGALRLE PLSKEYIQKS YKEPTEQFPE GKWRPVPLTV
310 320 330 340 350
SKGLSGGGYT YKITTPNGTV HERLWAYPEA SYQKLVADNL VYFGKDNGGI
360 370 380 390 400
PQRVMYAHHS KGQPTTNYWD NVASNKEGKK EILDLFGDNV FDTPKPTALL
410 420 430 440 450
KKIIKLAIDK DGVVLDFFAG SGTTAHAVMA LNEEDGGQRT FILCTIDQAL
460 470 480 490 500
SNNTIAKKAG YNTIDEISRE RITRVAAKIR ANNPATNSDL GFKHYRFATP
510 520 530 540 550
TQQTLDDLDS FDIATGHFIN TSGQLAAFTE SGFTDMINPF SARGLGVPGG
560 570 580 590 600
ASGEETLLTT WLVADGYKMD IDVQTVDFSG YCARYVDNTR LYLIDERWGT
610 620 630 640 650
EQTRDLLNHI GTHQLPVQTI VIYGYSFDLE SIRELEIGLK QLDQKVNLVK

RY
Length:652
Mass (Da):73,336
Last modified:January 23, 2002 - v2
Checksum:i385DE4851545C84E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551Missing (PubMed:8387444).Curated
Sequence conflicti126 – 1261A → S (PubMed:8387444).Curated
Sequence conflicti587 – 5882DN → ND (PubMed:8387444).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90544 Genomic DNA. No translation available.
AE006468 Genomic DNA. Translation: AAL19311.1.
PIRiJN0657.
RefSeqiNP_459352.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19311; AAL19311; STM0357.
GeneIDi1251876.
KEGGistm:STM0357.
PATRICi32379033. VBISalEnt20916_0378.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90544 Genomic DNA. No translation available.
AE006468 Genomic DNA. Translation: AAL19311.1.
PIRiJN0657.
RefSeqiNP_459352.1. NC_003197.1.

3D structure databases

ProteinModelPortaliP40814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM0357.

Protein family/group databases

REBASEi5598. M.StyLT2ORF357P.

Proteomic databases

PaxDbiP40814.
PRIDEiP40814.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19311; AAL19311; STM0357.
GeneIDi1251876.
KEGGistm:STM0357.
PATRICi32379033. VBISalEnt20916_0378.

Phylogenomic databases

eggNOGiCOG2189.
HOGENOMiHOG000253523.
KOiK07316.
OMAiPYSVFYQ.
OrthoDBiEOG6W9X8K.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-358-MONOMER.

Family and domain databases

Gene3Di3.40.50.150. 3 hits.
InterProiIPR002295. D21N6_MeTrfase.
IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PIRSFiPIRSF015855. TypeIII_Mtase_mKpnI. 1 hit.
PRINTSiPR00506. D21N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 3 hits.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the Salmonella typhimurium StyLT1 restriction-modification genes: homologies with EcoP1 and EcoP15 type-III R-M systems and presence of helicase domains."
    Dartois V., de Backer O., Colson C.
    Gene 127:105-110(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT7.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.

Entry informationi

Entry nameiT3MO_SALTY
AccessioniPrimary (citable) accession number: P40814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2002
Last modified: January 7, 2015
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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.