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P11409

- MTP2_PROHU

UniProt

P11409 - MTP2_PROHU

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Protein

Modification methylase PvuII

Gene

pvuIIM

Organism
Proteus hauseri
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

This methylase recognizes the double-stranded sequence CAGCTG, causes specific methylation on C-4 on both strands, and protects the DNA from cleavage by the PvuII endonuclease.

Catalytic activityi

S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N(4)-methylcytosine.

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. N-methyltransferase activity Source: InterPro
  3. site-specific DNA-methyltransferase (cytosine-N4-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

BRENDAi2.1.1.113. 5049.

Protein family/group databases

REBASEi3485. M.PvuII.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase PvuII (EC:2.1.1.113)
Short name:
M.PvuII
Alternative name(s):
N-4 cytosine-specific methyltransferase PvuII
Gene namesi
Name:pvuIIM
OrganismiProteus hauseri
Taxonomic identifieri183417 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Modification methylase PvuIIPRO_0000087931Add
BLAST

Structurei

Secondary structure

1
336
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243
Beta strandi26 – 338
Helixi35 – 384
Helixi39 – 413
Beta strandi47 – 526
Beta strandi57 – 593
Helixi68 – 8619
Beta strandi87 – 9711
Beta strandi105 – 1084
Helixi111 – 12111
Beta strandi126 – 1349
Helixi144 – 1485
Beta strandi157 – 16812
Helixi173 – 1753
Beta strandi221 – 2244
Helixi232 – 2409
Helixi253 – 26210
Beta strandi268 – 2714
Helixi278 – 2858
Beta strandi289 – 2957
Helixi297 – 3048
Helixi305 – 3073
Helixi314 – 32512

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOOX-ray2.80A14-336[»]
DisProtiDP00060.
ProteinModelPortaliP11409.
SMRiP11409. Positions 16-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11409.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati11 – 1131031Add
BLAST
Repeati181 – 2931132Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR002941. DNA_methylase_N4/N6.
IPR017985. MeTrfase_CN4_CS.
IPR001091. RM_Methylase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF01555. N6_N4_Mtase. 1 hit.
[Graphical view]
PRINTSiPR00508. S21N4MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00093. N4_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11409 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMTLNLQTMS SNDMLNFGKK PAYTTSNGSM YIGDSLELLE SFPDESISLV
60 70 80 90 100
MTSPPFALQR KKEYGNLEQH EYVDWFLSFA KVVNKKLKPD GSFVVDFGGA
110 120 130 140 150
YMKGVPARSI YNFRVLIRMI DEVGFFLAED FYWFNPSKLP SPIEWVNKRK
160 170 180 190 200
IRVKDAVNTV WWFSKTEWPK SDITKVLAPY SDRMKKLIED PDKFYTPKTR
210 220 230 240 250
PSGHDIGKSF SKDNGGSIPP NLLQISNSES NGQYLANCKL MGIKAHPARF
260 270 280 290 300
PAKLPEFFIR MLTEPDDLVV DIFGGSNTTG LVAERESRKW ISFEMKPEYV
310 320 330
AASAFRFLDN NISEEKITDI YNRILNGESL DLNSII
Length:336
Mass (Da):38,365
Last modified:October 1, 1996 - v2
Checksum:i084371A667F86B91
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441D → E in CAA32026. (PubMed:2662138)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13778 Genomic DNA. Translation: CAA32026.1.
AF305615 Genomic DNA. Translation: AAA96336.1.
PIRiS04739.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X13778 Genomic DNA. Translation: CAA32026.1 .
AF305615 Genomic DNA. Translation: AAA96336.1 .
PIRi S04739.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BOO X-ray 2.80 A 14-336 [» ]
DisProti DP00060.
ProteinModelPortali P11409.
SMRi P11409. Positions 16-335.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 3485. M.PvuII.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 2.1.1.113. 5049.

Miscellaneous databases

EvolutionaryTracei P11409.

Family and domain databases

Gene3Di 3.40.50.150. 2 hits.
InterProi IPR002941. DNA_methylase_N4/N6.
IPR017985. MeTrfase_CN4_CS.
IPR001091. RM_Methylase.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF01555. N6_N4_Mtase. 1 hit.
[Graphical view ]
PRINTSi PR00508. S21N4MTFRASE.
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS00093. N4_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence, internal homology and high-level expression of the gene for a DNA-(cytosine N4)-methyltransferase, M.Pvu II."
    Tao T., Walter J., Brennan K.J., Cotterman M.M., Blumenthal R.M.
    Nucleic Acids Res. 17:4161-4175(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.
  2. "Gene pvuIIW: a possible modulator of PvuII endonuclease subunit association."
    Adams G.M., Blumenthal R.M.
    Gene 157:193-199(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80, SEQUENCE REVISION TO 44.
    Strain: ATCC 13315 / DSM 30118 / JCM 1668 / NBRC 3851 / NCIMB 4175 / NCTC 4175 / NRRL B-3405.
  3. "Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment."
    Gong W., O'Gara M., Blumenthal R.M., Cheng X.
    Nucleic Acids Res. 25:2702-2715(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiMTP2_PROHU
AccessioniPrimary (citable) accession number: P11409
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: October 1, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Restriction enzymes and methylases
    Classification of restriction enzymes and methylases and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3