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Q89Z59

- T1M_BACTN

UniProt

Q89Z59 - T1M_BACTN

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Protein

Probable type I restriction enzyme BthVORF4518P M protein

Gene
BT_4518
Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei214 – 2141S-adenosyl-L-methionine

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. N-methyltransferase activity Source: InterPro
  3. site-specific DNA-methyltransferase (adenine-specific) activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciBTHE226186:GJXV-4599-MONOMER.

Protein family/group databases

REBASEi7071. M.BthVORF4518P.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable type I restriction enzyme BthVORF4518P M protein (EC:2.1.1.72)
Short name:
M.BthVORF4518P
Gene namesi
Ordered Locus Names:BT_4518
OrganismiBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifieri226186 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides
ProteomesiUP000001414: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 472472Probable type I restriction enzyme BthVORF4518P M proteinPRO_0000310988Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi226186.BT_4518.

Structurei

Secondary structure

1
472
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2414
Helixi29 – 5123
Helixi64 – 685
Helixi73 – 8715
Helixi91 – 966
Turni97 – 993
Helixi107 – 11812
Helixi128 – 14215
Turni145 – 1473
Helixi150 – 1523
Helixi156 – 16611
Beta strandi174 – 1763
Helixi183 – 19311
Helixi200 – 2078
Beta strandi210 – 2156
Helixi217 – 22913
Beta strandi238 – 2414
Turni244 – 2463
Beta strandi253 – 2586
Beta strandi277 – 2793
Helixi284 – 29512
Beta strandi296 – 30712
Helixi308 – 3125
Helixi316 – 32712
Beta strandi328 – 3358
Beta strandi338 – 3436
Beta strandi348 – 35710
Beta strandi360 – 3667
Beta strandi375 – 3784
Helixi382 – 3854
Helixi386 – 3938
Turni401 – 4033
Beta strandi408 – 4136
Helixi414 – 4196
Helixi421 – 4233

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OKCX-ray2.20A/B1-444[»]
ProteinModelPortaliQ89Z59.
SMRiQ89Z59. Positions 7-432.

Miscellaneous databases

EvolutionaryTraceiQ89Z59.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni151 – 1566S-adenosyl-L-methionine binding
Regioni181 – 1833S-adenosyl-L-methionine binding
Regioni243 – 2442S-adenosyl-L-methionine binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0286.
HOGENOMiHOG000295041.
KOiK03427.
OMAiCAGHVED.
OrthoDBiEOG686NCV.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00507. N12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q89Z59-1 [UniParc]FASTAAdd to Basket

« Hide

MATNSSTEQS LTKKVWNLAT TLAGQGIGFT DYITQLTYLL FLKMDAENVE    50
MFGEESAIPT GYQWADLIAF DGLDLVKQYE ETLKLLSELD NLIGTIYTKA 100
QNKIDKPVYL KKVITMIDEE QWLIMDGDVK GAIYESILEK NGQDKKSGAG 150
QYFTPRPLIQ AMVDCINPQM GETVCDPACG TGGFLLTAYD YMKGQSASKE 200
KRDFLRDKAL HGVDNTPLVV TLASMNLYLH GIGTDRSPIV CEDSLEKEPS 250
TLVDVILANP PFGTRPAGSV DINRPDFYVE TKNNQLNFLQ HMMLMLKTGG 300
RAAVVLPDNV LFEAGAGETI RKRLLQDFNL HTILRLPTGI FYAQGVKANV 350
LFFSKGQPTK EIWFYDYRTD IKHTLATNKL ERHHLDDFVS CYNNRVEIYD 400
AENNPQGRWR KYPVDEIIAR DKTSLDITWI KPGGEVDDRS LAELMADIKD 450
KSQTISRAVT ELEKLLANIE EN 472
Length:472
Mass (Da):53,127
Last modified:June 1, 2003 - v1
Checksum:i3891797D2845329D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015928 Genomic DNA. Translation: AAO79623.1.
RefSeqiNP_813429.1. NC_004663.1.
WP_011109305.1. NC_004663.1.

Genome annotation databases

EnsemblBacteriaiAAO79623; AAO79623; BT_4518.
GeneIDi1073274.
KEGGibth:BT_4518.
PATRICi21064114. VBIBacThe70966_4602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015928 Genomic DNA. Translation: AAO79623.1 .
RefSeqi NP_813429.1. NC_004663.1.
WP_011109305.1. NC_004663.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OKC X-ray 2.20 A/B 1-444 [» ]
ProteinModelPortali Q89Z59.
SMRi Q89Z59. Positions 7-432.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 226186.BT_4518.

Protein family/group databases

REBASEi 7071. M.BthVORF4518P.

Protocols and materials databases

DNASUi 1073274.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO79623 ; AAO79623 ; BT_4518 .
GeneIDi 1073274.
KEGGi bth:BT_4518.
PATRICi 21064114. VBIBacThe70966_4602.

Phylogenomic databases

eggNOGi COG0286.
HOGENOMi HOG000295041.
KOi K03427.
OMAi CAGHVED.
OrthoDBi EOG686NCV.

Enzyme and pathway databases

BioCyci BTHE226186:GJXV-4599-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q89Z59.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR022749. D12N6_MeTrfase_N.
IPR003356. DNA_methylase_A-5.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR002296. N12N6_MeTrfase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view ]
PRINTSi PR00507. N12N6MTFRASE.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiT1M_BACTN
AccessioniPrimary (citable) accession number: Q89Z59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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