Reviewed, UniProtKB/Swiss-Prot P34720 (MT1A_MORBO)

Names and origin

Protein names

Recommended name:
    Modification methylase MboIA
      Short name=M.MboIA
    EC=2.1.1.72
Alternative name(s):
    Adenine-specific methyltransferase MboIA

Gene names

Name:	mboIAM
Synonyms:	mboA

Organism

Moraxella bovis

Taxonomic identifier

476 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Moraxella

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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 activity	S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.
Miscellaneous	The MboI restriction system has two different methylases.
Sequence similarities	Belongs to the N(4)/N(6)-methyltransferase family.

Ontologies

Keywords
Biological process	Restriction system
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Gene Ontology (GO)
Biological process	DNA methylation Inferred from electronic annotation. Source: InterPro DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro site-specific DNA-methyltransferase (adenine-specific) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 294	294	Modification methylase MboIA		PRO_0000087955
Sites
	Binding site	7	1	S-adenosyl-L-methionine By similarity
	Binding site	11	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	61	1	S-adenosyl-L-methionine By similarity
	Binding site	198	1	S-adenosyl-L-methionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P34720-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: E042441B46C6BB04	FASTA	294	33,767
	10 20 30 40 50 60 MKPFIKWAGG KNSLLDEIQK RLPDFVHSQD FCLVEPFVGG GAVSLWALSD LPHLKQLVIN 70 80 90 100 110 120 DCNADLINVY QVIKNNPDDL IGYIENLQSH YDKLTDLESK KPYFYHKRDV FNQRTSNDIE 130 140 150 160 170 180 QAGLFIFLNK SAFNGLYRVN KNNQFNVPIG NYKKPTFVDK ENILNISKKL QNTKILSGDF 190 200 210 220 230 240 ELVLAHLPNN FPCLFYLDPP YRPISDTASF TSYSDNGFDD NEQKRLANFC KKIDKLGHYF 250 260 270 280 290 LLSNSDPKNT NSSDEFFDEL YQDFKIERIQ ANRTISANSN GRKKVNEIIV SNGV

References

[1]	"Gene structure and expression of the MboI restriction-modification system." Ueno T., Ito H., Kimizuka F., Kotani H., Nakajima K. Nucleic Acids Res. 21:2309-2313(1993) [PubMed: 8506128] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10900 / DSM 6328 / LMG 986 / NCTC 11013.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D13968 Genomic DNA. Translation: BAA03071.1.
PIR	S35646.
3D structure databases
HSSP	HSSP built from PDB template 2DPM based on UniProtKB P04043.
ModBase	Search...
Protein family/group databases
REBASE	3667. M1.MboI.
Enzyme and pathway databases
BRENDA	2.1.1.72. 96192.
Family and domain databases
InterPro	IPR002294. D12N6_MeTrfase. IPR012326. Dam. IPR002052. DNA_methylase_N6_adenine_CS. IPR012327. MeTrfase_D12. [Graphical view]
Pfam	PF02086. MethyltransfD12. 1 hit. [Graphical view]
PRINTS	PR00505. D12N6MTFRASE.
TIGRFAMs	TIGR00571. dam. 1 hit.
PROSITE	PS00092. N6_MTASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MT1A_MORBO

Accession

Primary (citable) accession number: P34720

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)