Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.72. 3416.

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000879671 – 260Modification methylase MboIIAdd BLAST260

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi12 – 18Combined sources7
Beta strandi24 – 29Combined sources6
Helixi39 – 41Combined sources3
Helixi46 – 63Combined sources18
Beta strandi64 – 74Combined sources11
Helixi76 – 88Combined sources13
Beta strandi92 – 99Combined sources8
Beta strandi109 – 111Combined sources3
Beta strandi117 – 125Combined sources9
Helixi132 – 134Combined sources3
Helixi141 – 151Combined sources11
Beta strandi170 – 173Combined sources4
Helixi199 – 209Combined sources11
Beta strandi215 – 220Combined sources6
Helixi225 – 232Combined sources8
Beta strandi236 – 242Combined sources7
Helixi244 – 255Combined sources12

3D structure databases

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

Protein family/group databases

REBASEi3441. M1.MboII.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.1.1.72. 3416.

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...

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: November 2, 2016
This is version 88 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

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 one 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.