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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: 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 + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei214S-adenosyl-L-methionine1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

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
Proteomesi
  • UP000001414 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003109881 – 472Probable type I restriction enzyme BthVORF4518P M proteinAdd BLAST472

Proteomic databases

PaxDbiQ89Z59.

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

1472
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 24Combined sources14
Helixi29 – 51Combined sources23
Helixi64 – 68Combined sources5
Helixi73 – 87Combined sources15
Helixi91 – 96Combined sources6
Turni97 – 99Combined sources3
Helixi107 – 118Combined sources12
Helixi128 – 142Combined sources15
Turni145 – 147Combined sources3
Helixi150 – 152Combined sources3
Helixi156 – 166Combined sources11
Beta strandi174 – 176Combined sources3
Helixi183 – 193Combined sources11
Helixi200 – 207Combined sources8
Beta strandi210 – 215Combined sources6
Helixi217 – 229Combined sources13
Beta strandi238 – 241Combined sources4
Turni244 – 246Combined sources3
Beta strandi253 – 258Combined sources6
Beta strandi277 – 279Combined sources3
Helixi284 – 295Combined sources12
Beta strandi296 – 307Combined sources12
Helixi308 – 312Combined sources5
Helixi316 – 327Combined sources12
Beta strandi328 – 335Combined sources8
Beta strandi338 – 343Combined sources6
Beta strandi348 – 357Combined sources10
Beta strandi360 – 366Combined sources7
Beta strandi375 – 378Combined sources4
Helixi382 – 385Combined sources4
Helixi386 – 393Combined sources8
Turni401 – 403Combined sources3
Beta strandi408 – 413Combined sources6
Helixi414 – 419Combined sources6
Helixi421 – 423Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OKCX-ray2.20A/B1-444[»]
ProteinModelPortaliQ89Z59.
SMRiQ89Z59.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ89Z59.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni151 – 156S-adenosyl-L-methionine binding6
Regioni181 – 183S-adenosyl-L-methionine binding3
Regioni243 – 244S-adenosyl-L-methionine binding2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CVR. Bacteria.
COG0286. LUCA.
HOGENOMiHOG000295041.
InParanoidiQ89Z59.
KOiK03427.
OMAiINYSDYV.
OrthoDBiPOG091H07S2.

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.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q89Z59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATNSSTEQS LTKKVWNLAT TLAGQGIGFT DYITQLTYLL FLKMDAENVE
60 70 80 90 100
MFGEESAIPT GYQWADLIAF DGLDLVKQYE ETLKLLSELD NLIGTIYTKA
110 120 130 140 150
QNKIDKPVYL KKVITMIDEE QWLIMDGDVK GAIYESILEK NGQDKKSGAG
160 170 180 190 200
QYFTPRPLIQ AMVDCINPQM GETVCDPACG TGGFLLTAYD YMKGQSASKE
210 220 230 240 250
KRDFLRDKAL HGVDNTPLVV TLASMNLYLH GIGTDRSPIV CEDSLEKEPS
260 270 280 290 300
TLVDVILANP PFGTRPAGSV DINRPDFYVE TKNNQLNFLQ HMMLMLKTGG
310 320 330 340 350
RAAVVLPDNV LFEAGAGETI RKRLLQDFNL HTILRLPTGI FYAQGVKANV
360 370 380 390 400
LFFSKGQPTK EIWFYDYRTD IKHTLATNKL ERHHLDDFVS CYNNRVEIYD
410 420 430 440 450
AENNPQGRWR KYPVDEIIAR DKTSLDITWI KPGGEVDDRS LAELMADIKD
460 470
KSQTISRAVT ELEKLLANIE EN
Length:472
Mass (Da):53,127
Last modified:June 1, 2003 - v1
Checksum:i3891797D2845329D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE015928 Genomic DNA. Translation: AAO79623.1.
RefSeqiNP_813429.1. NC_004663.1.
WP_011109305.1. NC_004663.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OKCX-ray2.20A/B1-444[»]
ProteinModelPortaliQ89Z59.
SMRiQ89Z59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226186.BT_4518.

Protein family/group databases

REBASEi7071. M.BthVORF4518P.

Proteomic databases

PaxDbiQ89Z59.

Protocols and materials databases

DNASUi1073274.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CVR. Bacteria.
COG0286. LUCA.
HOGENOMiHOG000295041.
InParanoidiQ89Z59.
KOiK03427.
OMAiINYSDYV.
OrthoDBiPOG091H07S2.

Miscellaneous databases

EvolutionaryTraceiQ89Z59.

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.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF12161. HsdM_N. 1 hit.
PF02384. N6_Mtase. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 95 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.