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P50196

- MTE8_ECOLX

UniProt

P50196 - MTE8_ECOLX

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Protein

Modification methylase Eco47II

Gene

eco47IIM

Organism
Escherichia coli
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

This methylase recognizes the double-stranded sequence GGNCC, causes specific methylation on C-? on both strands, and protects the DNA from cleavage by the Eco47II endonuclease.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531PROSITE-ProRule annotation

GO - Molecular functioni

  1. DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB-EC
  2. DNA binding Source: InterPro

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

S-adenosyl-L-methionine

Protein family/group databases

REBASEi3372. M.Eco47II.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase Eco47II (EC:2.1.1.37)
Short name:
M.Eco47II
Alternative name(s):
Cytosine-specific methyltransferase Eco47II
Gene namesi
Name:eco47IIM
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 417417Modification methylase Eco47IIPRO_0000087875Add
BLAST

Proteomic databases

PRIDEiP50196.

Structurei

3D structure databases

ProteinModelPortaliP50196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 414334SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR009061. DNA-bd_dom_put.
IPR000551. MerR-type_HTH_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR10629. PTHR10629. 1 hit.
PfamiPF00145. DNA_methylase. 1 hit.
PF00376. MerR. 1 hit.
[Graphical view]
PRINTSiPR00105. C5METTRFRASE.
SUPFAMiSSF46955. SSF46955. 1 hit.
SSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00675. dcm. 1 hit.
PROSITEiPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50196-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLAWLLNMLK EEFSLSEVAD ILGVSKETLR RWDTAGKLVS QRNDENNYRF
60 70 80 90 100
YKKEQLKNFE QAQFLFKSQW PDETKISNNV YTVLELFAGA GGMALGLEKA
110 120 130 140 150
GLKSVLLNEI DSHACKTLRK NRPEWNVVEG DVSQVDFTPY RNTVDVLAGG
160 170 180 190 200
FPCQAFSYAG KKLGFEDTRG TLFFEFARAA KEINPKVLLA ENVRGLLNHD
210 220 230 240 250
AGRTLETIKN IITDLGYTLF EPRVLKAIFY KVPQKRERLI IVAVRNDLAD
260 270 280 290 300
GIDYEWPSSY NKILTLKDAL KKGELYDSDV PESEGQKYPK RKAEILSMVP
310 320 330 340 350
PGGYWRDLPE DIQKEYMLKS FYLGGGKTGM ARRLSWDEPS LTLTCAPAQK
360 370 380 390 400
QTERCHPEET RPLTVREYAR IQTFPDEWVF EGPMSAKYKQ IGNAVPVNLS
410
FAVGKSVVHL LDKINKR
Length:417
Mass (Da):47,513
Last modified:October 1, 1996 - v1
Checksum:iC399A49E00BDAFD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82105 Genomic DNA. Translation: CAA57629.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82105 Genomic DNA. Translation: CAA57629.1 .

3D structure databases

ProteinModelPortali P50196.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 3372. M.Eco47II.

Proteomic databases

PRIDEi P50196.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR009061. DNA-bd_dom_put.
IPR000551. MerR-type_HTH_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR10629. PTHR10629. 1 hit.
Pfami PF00145. DNA_methylase. 1 hit.
PF00376. MerR. 1 hit.
[Graphical view ]
PRINTSi PR00105. C5METTRFRASE.
SUPFAMi SSF46955. SSF46955. 1 hit.
SSF53335. SSF53335. 1 hit.
TIGRFAMsi TIGR00675. dcm. 1 hit.
PROSITEi PS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterization of the unusual restriction-modification system comprising two restriction endonucleases and one methyltransferase."
    Stankevicius K., Povilionis P., Lubys A., Menkevicius S., Janulaitis A.
    Gene 157:49-53(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: RFL47.

Entry informationi

Entry nameiMTE8_ECOLX
AccessioniPrimary (citable) accession number: P50196
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 1, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3