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P23192

- MTM2_MORBO

UniProt

P23192 - MTM2_MORBO

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Protein
Modification methylase MboII
Gene
mboIIM
Organism
Moraxella bovis
Status
Reviewed - 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 MboII
PRO_0000087967Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G60X-ray1.74A/B1-260[»]
ProteinModelPortaliP23192.
SMRiP23192. Positions 1-256.

Miscellaneous databases

EvolutionaryTraceiP23192.

Family & Domainsi

Sequence similaritiesi

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-like.
[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

MLEINKIHQM NCFDFLDQVE NKSVQLAVID PPYNLSKADW DSFDSHNEFL    50
PFTYRWIDKV LDKLDKDGSL YIFNTPFNCA FICQYLVSKG MIFQNWITWD 100
KRDGMGSAKR GFSTGQETIL FFSKSKNHTF NYDEVRVPYE STDRIKHASE 150
KGILKNGKRW FPNPNGRLCG EVWHFSSQRH KEKVNGKTVK LTHITPKPRD 200
LIERIIRASS NPNDLVLDCF MGSGTTAIVA KKLGRNFIGC DMNAEYVNQA 250
NFVLNQLEIN 260
Length:260
Mass (Da):30,077
Last modified:November 1, 1991 - v1
Checksum:iE53354DCA12DBE7C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56977 Genomic DNA. Translation: CAA40297.1.
PIRiS26835.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56977 Genomic DNA. Translation: CAA40297.1 .
PIRi S26835.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G60 X-ray 1.74 A/B 1-260 [» ]
ProteinModelPortali P23192.
SMRi P23192. Positions 1-256.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 3441. M1.MboII.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P23192.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR002941. DNA_methylase_N4/N6.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR001091. RM_Methylase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF01555. N6_N4_Mtase. 1 hit.
[Graphical view ]
PRINTSi PR00508. S21N4MTFRASE.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 78 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

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