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Q89Z59 (T1M_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable type I restriction enzyme BthVORF4518P M protein
Short name=M.BthVORF4518P
EC=2.1.1.72
Gene names
Ordered Locus Names:BT_4518
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides ›

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Methylation of specific adenine residues; required for both restriction and modification activities By similarity.

Catalytic activity

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

Subunit structure

The type I restriction/modification system is composed of three polypeptides R, M and S By similarity.

Miscellaneous

Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and Mg2+ as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Probable type I restriction enzyme BthVORF4518P M protein
PRO_0000310988

Regions

Region151 – 1566S-adenosyl-L-methionine binding
Region181 – 1833S-adenosyl-L-methionine binding
Region243 – 2442S-adenosyl-L-methionine binding

Sites

Binding site2141S-adenosyl-L-methionine

Secondary structure

1 ................................................................. 472
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q89Z59 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 3891797D2845329D

FASTA47253,127
        10         20         30         40         50         60 
MATNSSTEQS LTKKVWNLAT TLAGQGIGFT DYITQLTYLL FLKMDAENVE MFGEESAIPT 

        70         80         90        100        110        120 
GYQWADLIAF DGLDLVKQYE ETLKLLSELD NLIGTIYTKA QNKIDKPVYL KKVITMIDEE 

       130        140        150        160        170        180 
QWLIMDGDVK GAIYESILEK NGQDKKSGAG QYFTPRPLIQ AMVDCINPQM GETVCDPACG 

       190        200        210        220        230        240 
TGGFLLTAYD YMKGQSASKE KRDFLRDKAL HGVDNTPLVV TLASMNLYLH GIGTDRSPIV 

       250        260        270        280        290        300 
CEDSLEKEPS TLVDVILANP PFGTRPAGSV DINRPDFYVE TKNNQLNFLQ HMMLMLKTGG 

       310        320        330        340        350        360 
RAAVVLPDNV LFEAGAGETI RKRLLQDFNL HTILRLPTGI FYAQGVKANV LFFSKGQPTK 

       370        380        390        400        410        420 
EIWFYDYRTD IKHTLATNKL ERHHLDDFVS CYNNRVEIYD AENNPQGRWR KYPVDEIIAR 

       430        440        450        460        470 
DKTSLDITWI KPGGEVDDRS LAELMADIKD KSQTISRAVT ELEKLLANIE EN

« Hide

References

« Hide 'large scale' references
[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.
[2]"Crystal structure of type I restriction enzyme protein (NP_813429.1) from bacteriodes thetaiotaomicron VPI-5482 at 2.20 A resolution resolution."
Joint center for structural genomics (JCSG)
Submitted (JAN-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015928 Genomic DNA. Translation: AAO79623.1.
RefSeqNP_813429.1. NC_004663.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OKCX-ray2.20A/B1-444[»]
ProteinModelPortalQ89Z59.
SMRQ89Z59. Positions 7-432.
ModBaseSearch...

Protein-protein interaction databases

STRING226186.BT_4518.

Protein family/group databases

REBASE7071. M.BthVORF4518P.

Protocols and materials databases

DNASU1073274.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO79623; AAO79623; BT_4518.
GeneID1073274.
KEGGbth:BT_4518.
PATRIC21064114. VBIBacThe70966_4602.

Phylogenomic databases

eggNOGCOG0286.
HOGENOMHOG000295041.
KOK03427.
OMAIVQKLWN.
ProtClustDBCLSK823977.

Enzyme and pathway databases

BioCycBTHE226186:GJXV-4599-MONOMER.

Family and domain databases

InterProIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
[Graphical view]
PfamPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSPR00507. N12N6MTFRASE.
PROSITEPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ89Z59.

Entry information

Entry nameT1M_BACTN
AccessionPrimary (citable) accession number: Q89Z59
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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