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Protein

Modification methylase MboIA

Gene

mboIAM

Organism
Moraxella bovis
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

This methylase recognizes the double-stranded sequence GATC, causes specific methylation on A-2 on both strands, and protects the DNA from cleavage by the MboI endonuclease.

Catalytic activityi

S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei7S-adenosyl-L-methionineBy similarity1
Binding sitei11S-adenosyl-L-methionine; via amide nitrogenBy similarity1
Binding sitei61S-adenosyl-L-methionineBy similarity1
Binding sitei198S-adenosyl-L-methionineBy similarity1

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

Protein family/group databases

REBASEi3667. M1.MboI.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase MboIA (EC:2.1.1.72)
Short name:
M.MboIA
Alternative name(s):
Adenine-specific methyltransferase MboIA
Gene namesi
Name:mboIAM
Synonyms:mboA
OrganismiMoraxella bovis
Taxonomic identifieri476 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeMoraxella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000879551 – 294Modification methylase MboIAAdd BLAST294

Structurei

3D structure databases

ProteinModelPortaliP34720.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

Gene3Di1.10.1020.10. 1 hit.
3.40.50.150. 2 hits.
InterProiIPR023095. Ade_MeTrfase_dom_2.
IPR012263. M_m6A_EcoRV.
IPR012327. MeTrfase_D12.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF02086. MethyltransfD12. 1 hit.
[Graphical view]
PIRSFiPIRSF000398. M_m6A_EcoRV. 1 hit.
PRINTSiPR00505. D12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00571. dam. 1 hit.

Sequencei

Sequence statusi: Complete.

P34720-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPFIKWAGG KNSLLDEIQK RLPDFVHSQD FCLVEPFVGG GAVSLWALSD
60 70 80 90 100
LPHLKQLVIN DCNADLINVY QVIKNNPDDL IGYIENLQSH YDKLTDLESK
110 120 130 140 150
KPYFYHKRDV FNQRTSNDIE QAGLFIFLNK SAFNGLYRVN KNNQFNVPIG
160 170 180 190 200
NYKKPTFVDK ENILNISKKL QNTKILSGDF ELVLAHLPNN FPCLFYLDPP
210 220 230 240 250
YRPISDTASF TSYSDNGFDD NEQKRLANFC KKIDKLGHYF LLSNSDPKNT
260 270 280 290
NSSDEFFDEL YQDFKIERIQ ANRTISANSN GRKKVNEIIV SNGV
Length:294
Mass (Da):33,767
Last modified:February 1, 1994 - v1
Checksum:iE042441B46C6BB04
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13968 Genomic DNA. Translation: BAA03071.1.
PIRiS35646.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13968 Genomic DNA. Translation: BAA03071.1.
PIRiS35646.

3D structure databases

ProteinModelPortaliP34720.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi3667. M1.MboI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.1020.10. 1 hit.
3.40.50.150. 2 hits.
InterProiIPR023095. Ade_MeTrfase_dom_2.
IPR012263. M_m6A_EcoRV.
IPR012327. MeTrfase_D12.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF02086. MethyltransfD12. 1 hit.
[Graphical view]
PIRSFiPIRSF000398. M_m6A_EcoRV. 1 hit.
PRINTSiPR00505. D12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00571. dam. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMT1A_MORBO
AccessioniPrimary (citable) accession number: P34720
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 7, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The MboI restriction system has two different methylases.

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

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.