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P12364

- T3MO_ECOLX

UniProt

P12364 - T3MO_ECOLX

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Protein

Type III restriction-modification system EcoP15I enzyme mod

Gene

mod

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

Functioni

Binds the system-specific DNA recognition site 5'-CAGCAC-3'. Necessary for both restriction and methylation (of one of the two A's).

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

Protein family/group databases

REBASEi3389. M.EcoP15I.

Names & Taxonomyi

Protein namesi
Recommended name:
Type III restriction-modification system EcoP15I enzyme mod (EC:2.1.1.72)
Short name:
M.EcoP15I
Alternative name(s):
EcoP15I methyltransferase
Gene namesi
Name:mod
Encoded oniPlasmid p15B0 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 645645Type III restriction-modification system EcoP15I enzyme modPRO_0000088031Add
BLAST

Proteomic databases

PRIDEiP12364.

Interactioni

Subunit structurei

Contains two different subunits: res and mod. Mod is a homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP12364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni123 – 1264Binding of S-adenosyl methionineSequence Analysis

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR002295. D21N6_MeTrfase.
IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR029063. SAM-dependent_MTases-like.
[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.

P12364-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKETIFSEV ETANSKQLAV LKANFPQCFD KNGAFIQEKL LEIIRASEVE
60 70 80 90 100
LSKESYSLNW LGKSYARLLA NLPPKTLLAE DKTHNQQEEN KNSQHLLIKG
110 120 130 140 150
DNLEVLKHMV NAYAEKVKMI YIDPPYNTGK DGFVYNDDRK FTPEQLSELA
160 170 180 190 200
GIDLDQAKRI LEFTTKGSSS HSAWLTFIYP RLYIARELMR EDGTIFISID
210 220 230 240 250
HNEFSQLKLV CDEIFGEQNH VGDLVWKNAT DNNPSNIAVE HEYIIVYTKN
260 270 280 290 300
KEQLISEWKS NISDVKNLLV NIGEEFASKY TGNELQEKYT QWFREHRSEL
310 320 330 340 350
WPLDRYKYID KDGIYTGSQS VHNPGKEGYR YDIIHPKTKK PCKQQPLMGY
360 370 380 390 400
RFPLDTMDRL LSEEKIIFGD DENKIIELKV YAKDYKQKLS SVIHLDGRVA
410 420 430 440 450
TNELKELFPE MTQPFTNAKT IKLVEDLISF ACDGEGIVLD FFAGSGTTAH
460 470 480 490 500
TVFNLNNKNK TSYQFITVQL DEPKKDKSDA MKHGYNTIFD LTKERLIRAS
510 520 530 540 550
KKNRDQGFKV YQLMADFRAK DESELTLSNH TFFDDVVLTP EQYDTLLTTW
560 570 580 590 600
CLYDGSLLTT PIEDVDLGGY KAHLCDGRLY LIAPNFTSEA LKALLQKVDS
610 620 630 640
DKDFAPNKVV FYGSNFESAK QMELNEALKS YANKKSIELD LVVRN
Length:645
Mass (Da):74,222
Last modified:October 1, 1989 - v1
Checksum:i0EFE6653BAA3A705
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06288 Genomic DNA. Translation: CAA29616.1.
PIRiS03208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06288 Genomic DNA. Translation: CAA29616.1 .
PIRi S03208.

3D structure databases

ProteinModelPortali P12364.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 3389. M.EcoP15I.

Proteomic databases

PRIDEi P12364.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.150. 2 hits.
InterProi IPR002295. D21N6_MeTrfase.
IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF01555. N6_N4_Mtase. 1 hit.
[Graphical view ]
PIRSFi PIRSF015855. TypeIII_Mtase_mKpnI. 1 hit.
PRINTSi PR00506. D21N6MTFRASE.
SUPFAMi SSF53335. SSF53335. 3 hits.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Type III DNA restriction and modification systems EcoP1 and EcoP15. Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1 mod mutants."
    Huembelin M., Suri B., Rao D.N., Hornby D.P., Eberle H., Pripfl T., Kenel S., Bickle T.A.
    J. Mol. Biol. 200:23-29(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiT3MO_ECOLX
AccessioniPrimary (citable) accession number: P12364
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 1, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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