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Reviewed, UniProtKB/Swiss-Prot P25201 (MTA1_ACICA)

Last modified September 22, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Modification methylase AccI
      Short name=M.AccI
    EC=2.1.1.72
Alternative name(s):
    Adenine-specific methyltransferase AccI
Gene names
Name: accIM
OrganismAcinetobacter calcoaceticus
Taxonomic identifier471 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

This methylase recognizes the double-stranded sequence GTMKAC, causes specific methylation on A-5 on both strands, and protects the DNA from cleavage by the AccI endonuclease.

Catalytic activity

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

Subunit structure

Monomer.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540Modification methylase AccI
PRO_0000087941

Sequences

Sequence LengthMass (Da)Tools
P25201-1 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: A2569693712E0F59

FASTA54063,093
        10         20         30         40         50         60 
MIKTTEHIVN NSIERDYSKS ISLEHRKKFA QFFTPFPIAY AMAKWILGNK QLKTVLEPAF 

        70         80         90        100        110        120 
GLGVFSRAIL SQQKEINIKA FEVDETIFEN AKEYFDDFEN VNILLQDYMY NDWKNKYDGI 

       130        140        150        160        170        180 
ICNPPYFKFH DYDNKNILKE IETNLKCKLN GFTNLYTLFL LKSIHQLSQN GRCAYIIPSE 

       190        200        210        220        230        240 
FLNSDYGKLV KTYLIKSKTL RHIIVIDFEE NVFDDALTTA SIILCANDNI TDKVQFNNIQ 

       250        260        270        280        290        300 
SLQDLSKIDE IINKYPNFLE TEQTYNFSDL NPEIKWKAYY QKQNSIKFKN LVPFSTYAKV 

       310        320        330        340        350        360 
VRGIATGSNE YFTFNLSKAK EFNIDEQYLL PCICSAKDAK TSFFTKQDFE ELKKSDKSVF 

       370        380        390        400        410        420 
LFNAQNSTDK NISSYIQKGE SEEINKRFLT ASRTPWYSLE NRKPAPIWVS VFNRSGLRFI 

       430        440        450        460        470        480 
RNEANISNLT SYHCIIQNKQ VVSEIDIDLL FAYLLTDTAK QIFEDNSRQY GNGLQKFEPN 

       490        500        510        520        530        540 
DLNKGMMLDL GLLDKQTSDE ILNLYKEYKY LILDNKNGDE IINKIDKILT DKYSEKKHWA 

« Hide

References

[1]"Cloning and nucleotide sequences of the AccI restriction-modification genes in Acinetobacter calcoaceticus."
Kawakami B., Hilzheber C., Nagatomo M., Oka M.
Agric. Biol. Chem. 55:1553-1559(1991) [PubMed: 1368703] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 49823.

Cross-references

Sequence databases

D10671 Genomic DNA. Translation: BAA01523.1.
PIRJU0470.

3D structure databases

ModBaseSearch...

Protein family/group databases

REBASE3271. M.AccI.

Enzyme and pathway databases

BRENDA2.1.1.72. 412.

Family and domain databases

InterProIPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
[Graphical view]
PRINTSPR00507. N12N6MTFRASE.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMTA1_ACICA
AccessionPrimary (citable) accession number: P25201
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 1, 1993
Last modified: September 22, 2009
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Restriction enzymes and methylases

Classification of restriction enzymes and methylases and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents