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Protein

Modification methylase PvuII

Gene

pvuIIM

Organism
Proteus hauseri
Status
Reviewed-Annotation score: 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 N4-methylcytosine.

GO - Molecular functioni

  • DNA binding Source: InterPro
  • N-methyltransferase activity Source: CAFA
  • site-specific DNA-methyltransferase (cytosine-N4-specific) activity Source: CAFA

GO - Biological processi

  • DNA methylation on adenine Source: CAFA
  • DNA restriction-modification system Source: UniProtKB-KW
  • N-4 methylation of cytosine Source: CAFA

Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processRestriction system
LigandS-adenosyl-L-methionine

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaeProteus

Pathology & Biotechi

Chemistry databases

DrugBankiDB01752. S-Adenosyl-L-Homocysteine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000879311 – 336Modification methylase PvuIIAdd BLAST336

Structurei

Secondary structure

1336
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 24Combined sources3
Beta strandi26 – 33Combined sources8
Helixi35 – 38Combined sources4
Helixi39 – 41Combined sources3
Beta strandi47 – 52Combined sources6
Beta strandi57 – 59Combined sources3
Helixi68 – 86Combined sources19
Beta strandi87 – 97Combined sources11
Beta strandi105 – 108Combined sources4
Helixi111 – 121Combined sources11
Beta strandi126 – 134Combined sources9
Helixi144 – 148Combined sources5
Beta strandi157 – 168Combined sources12
Helixi173 – 175Combined sources3
Beta strandi221 – 224Combined sources4
Helixi232 – 240Combined sources9
Helixi253 – 262Combined sources10
Beta strandi268 – 271Combined sources4
Helixi278 – 285Combined sources8
Beta strandi289 – 295Combined sources7
Helixi297 – 304Combined sources8
Helixi305 – 307Combined sources3
Helixi314 – 325Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BOOX-ray2.80A14-336[»]
DisProtiDP00060.
ProteinModelPortaliP11409.
SMRiP11409.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11409.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati11 – 1131Add BLAST103
Repeati181 – 2932Add BLAST113

Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

InterProiView protein in InterPro
IPR002941. DNA_methylase_N4/N6.
IPR017985. MeTrfase_CN4_CS.
IPR001091. RM_Methylase.
IPR029063. SAM-dependent_MTases.
PfamiView protein in Pfam
PF01555. N6_N4_Mtase. 1 hit.
PRINTSiPR00508. S21N4MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiView protein in PROSITE
PS00093. N4_MTASE. 1 hit.

Sequencei

Sequence statusi: Complete.

P11409-1 [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)DescriptionActionsGraphical viewLength
Sequence conflicti44D → E in CAA32026 (PubMed:2662138).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13778 Genomic DNA. Translation: CAA32026.1.
AF305615 Genomic DNA. Translation: AAA96336.1.
PIRiS04739.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13778 Genomic DNA. Translation: CAA32026.1.
AF305615 Genomic DNA. Translation: AAA96336.1.
PIRiS04739.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BOOX-ray2.80A14-336[»]
DisProtiDP00060.
ProteinModelPortaliP11409.
SMRiP11409.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB01752. S-Adenosyl-L-Homocysteine.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP11409.

Family and domain databases

InterProiView protein in InterPro
IPR002941. DNA_methylase_N4/N6.
IPR017985. MeTrfase_CN4_CS.
IPR001091. RM_Methylase.
IPR029063. SAM-dependent_MTases.
PfamiView protein in Pfam
PF01555. N6_N4_Mtase. 1 hit.
PRINTSiPR00508. S21N4MTFRASE.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiView protein in PROSITE
PS00093. N4_MTASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMTP2_PROHU
AccessioniPrimary (citable) accession number: P11409
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: May 10, 2017
This is version 111 of the entry and version 2 of the sequence. See 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

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.