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P34882 (MTAA_SYNP2) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Modification methylase AquI subunit alpha

Short name=M.AquI subunit alpha
Short name=M.AquiA
EC=2.1.1.37
Alternative name(s):
Cytosine-specific methyltransferase AquI subunit alpha
Gene names
Name:aquIMA
Synonyms:dcm
Ordered Locus Names:SYNPCC7002_A1188
OrganismSynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) [Complete proteome] [HAMAP]
Taxonomic identifier32049 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence CYCGRG, causes specific methylation on C-1 on both strands, and protects the DNA from cleavage by the AquI endonuclease.

Catalytic activity

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.

Subunit structure

Heterodimer of an alpha and a beta subunit.

Domain

Corresponds to the N-terminal half of the enzymatic domain.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Contains 1 SAM-dependent MTase C5-type domain.

Ontologies

Keywords
   Biological processRestriction system
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA restriction-modification system

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA (cytosine-5-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Modification methylase AquI subunit alpha
PRO_0000087854

Regions

Domain3 – 248246SAM-dependent MTase C5-type

Sites

Active site821 By similarity

Sequences

Sequence LengthMass (Da)Tools
P34882 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: FFF6B42B0997D82F

FASTA24827,161
        10         20         30         40         50         60 
MEKKLISLFS GAGGMDIGFH AAGFSTAVAV EQDPSCCNTL RLNMPDTPVI EGDITSITTQ 

        70         80         90        100        110        120 
VILEAAKVNP LEIDLVIGGP PCQSFSLAGK RMGMDDPRGM LVLEFLRVVR EALPKCFVME 

       130        140        150        160        170        180 
NVKGMINWSK GKALEAIMTE ASQPIKYAGK EYKYAVSYHV LNAADFGVPQ FRERVFIVGN 

       190        200        210        220        230        240 
RLGKTFQFPE PTHGPSNQAR QIDLFGKQLK PYKTVQDAIS TLPPATPPSA MALRVSQTIK 


DRIKNHGY 

« Hide

References

« Hide 'large scale' references
[1]"Agmenellum quadruplicatum M.AquI, a novel modification methylase."
Karreman C., de Waard A.
J. Bacteriol. 172:266-272(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Synechococcus sp. PCC 7002."
Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27264 / PCC 7002 / PR-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28051 Genomic DNA. Translation: AAA22067.1.
CP000951 Genomic DNA. Translation: ACA99187.1.
RefSeqYP_001734443.1. NC_010475.1.

3D structure databases

ProteinModelPortalP34882.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING32049.SYNPCC7002_A1188.

Protein family/group databases

REBASE3283. M.AquI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA99187; ACA99187; SYNPCC7002_A1188.
GeneID6056178.
KEGGsyp:SYNPCC7002_A1188.
PATRIC23816916. VBISynSp37135_1410.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0270.
KOK00558.
OMAEWNCISA.
OrthoDBEOG6M3PC7.

Enzyme and pathway databases

BioCycSSP32049:GKF7-1188-MONOMER.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR10629. PTHR10629. 1 hit.
PfamPF00145. DNA_methylase. 1 hit.
[Graphical view]
PRINTSPR00105. C5METTRFRASE.
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00675. dcm. 1 hit.
PROSITEPS00094. C5_MTASE_1. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTAA_SYNP2
AccessionPrimary (citable) accession number: P34882
Secondary accession number(s): B1XKE1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 11, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries