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Protein

Modification methylase MboII

Gene

mboIIM

Organism
Moraxella bovis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This methylase recognizes the double-stranded sequence GAAGA, causes specific methylation on A-5, and protects the DNA from cleavage by the MboII endonuclease. It is not known if the cytosine of the complementary sequence TCTTC is also methylated by this enzyme.

Catalytic activityi

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

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

Protein family/group databases

REBASEi3441. M1.MboII.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase MboII (EC:2.1.1.72)
Short name:
M.MboII
Alternative name(s):
Adenine-specific methyltransferase MboII
DNA MTase MboIIA
Gene namesi
Name:mboIIM
OrganismiMoraxella bovis
Taxonomic identifieri476 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeMoraxella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 260260Modification methylase MboIIPRO_0000087967Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
260
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi12 – 187Combined sources
Beta strandi24 – 296Combined sources
Helixi39 – 413Combined sources
Helixi46 – 6318Combined sources
Beta strandi64 – 7411Combined sources
Helixi76 – 8813Combined sources
Beta strandi92 – 998Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi117 – 1259Combined sources
Helixi132 – 1343Combined sources
Helixi141 – 15111Combined sources
Beta strandi170 – 1734Combined sources
Helixi199 – 20911Combined sources
Beta strandi215 – 2206Combined sources
Helixi225 – 2328Combined sources
Beta strandi236 – 2427Combined sources
Helixi244 – 25512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G60X-ray1.74A/B1-260[»]
ProteinModelPortaliP23192.
SMRiP23192. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23192.

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR001091. RM_Methylase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00508. S21N4MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23192-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEINKIHQM NCFDFLDQVE NKSVQLAVID PPYNLSKADW DSFDSHNEFL
60 70 80 90 100
PFTYRWIDKV LDKLDKDGSL YIFNTPFNCA FICQYLVSKG MIFQNWITWD
110 120 130 140 150
KRDGMGSAKR GFSTGQETIL FFSKSKNHTF NYDEVRVPYE STDRIKHASE
160 170 180 190 200
KGILKNGKRW FPNPNGRLCG EVWHFSSQRH KEKVNGKTVK LTHITPKPRD
210 220 230 240 250
LIERIIRASS NPNDLVLDCF MGSGTTAIVA KKLGRNFIGC DMNAEYVNQA
260
NFVLNQLEIN
Length:260
Mass (Da):30,077
Last modified:November 1, 1991 - v1
Checksum:iE53354DCA12DBE7C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56977 Genomic DNA. Translation: CAA40297.1.
PIRiS26835.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56977 Genomic DNA. Translation: CAA40297.1.
PIRiS26835.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G60X-ray1.74A/B1-260[»]
ProteinModelPortaliP23192.
SMRiP23192. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi3441. M1.MboII.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23192.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR001091. RM_Methylase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00508. S21N4MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of the MboII restriction-modification system."
    Bocklage H., Heeger K., Mueller-Hill B.
    Nucleic Acids Res. 19:1007-1013(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 10900 / DSM 6328 / LMG 986 / NCTC 11013.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS).

Entry informationi

Entry nameiMTM2_MORBO
AccessioniPrimary (citable) accession number: P23192
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: January 7, 2015
This is version 81 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  3. 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.