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Protein

Modification methylase SsoII

Gene

ssoIIM

Organism
Shigella sonnei
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

This methylase recognizes the double-stranded sequence CCNGG, causes specific methylation on C-2 on both strands, and protects the DNA from cleavage by the SsoII 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 sitei142 – 1421PROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Restriction system, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, S-adenosyl-L-methionine

Protein family/group databases

REBASEi3509. M.SsoII.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase SsoII (EC:2.1.1.37)
Short name:
M.SsoII
Alternative name(s):
Cytosine-specific methyltransferase SsoII
Gene namesi
Name:ssoIIM
Encoded oniPlasmid P40 Publication
OrganismiShigella sonnei
Taxonomic identifieri624 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Modification methylase SsoIIPRO_0000087906Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP34879.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 6658HTH cro/C1-typePROSITE-ProRule annotationAdd
BLAST
Domaini72 – 379308SAM-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 HTH cro/C1-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01381. HTH_3. 1 hit.
[Graphical view]
PRINTSiPR00105. C5METTRFRASE.
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00675. dcm. 1 hit.
PROSITEiPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS50943. HTH_CROC1. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P34879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDNIAATIK EKRERLHMTQ KEFADALGLS KYGDRTIRRW ERGETKPTGA
60 70 80 90 100
ELKAVIDFPD TPPYPNNENG RYRMIDLFAG IGGTRLGFHQ TNAVNVVFSS
110 120 130 140 150
EWDKFAQKTY HANYGDFPDG DITKIDEKDI PDHEILVGGF PCVAFSQAGL
160 170 180 190 200
KKGFNDTRGT LFFDIARIIK EKKPHAFLLE NVKNLLGHDK GRTFSIIKNT
210 220 230 240 250
LEELNYTVYY NIFAAKDFGV PQNRERIYIV GFNKEKVRNH EHFTFPTPLK
260 270 280 290 300
TKTRVGDILE KSVDNKYTLS DALWNGHQRR KLVNAAAGKG FGYGLFNENS
310 320 330 340 350
PYTNTISARY YKDGSEILIE QKGSNPRKIT PREASRLQGF PSDFIIPVSD
360 370
TQAYKQFGNS VAVPVINAIA EKIISTLDS
Length:379
Mass (Da):42,890
Last modified:February 1, 1994 - v1
Checksum:i97440A79FC6AB275
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86545 Genomic DNA. Translation: AAA98279.1.
PIRiJT0744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86545 Genomic DNA. Translation: AAA98279.1.
PIRiJT0744.

3D structure databases

ProteinModelPortaliP34879.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi3509. M.SsoII.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR001387. Cro/C1-type_HTH.
IPR010982. Lambda_DNA-bd_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01381. HTH_3. 1 hit.
[Graphical view]
PRINTSiPR00105. C5METTRFRASE.
SMARTiSM00530. HTH_XRE. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00675. dcm. 1 hit.
PROSITEiPS00094. C5_MTASE_1. 1 hit.
PS00095. C5_MTASE_2. 1 hit.
PS50943. HTH_CROC1. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Analysis of the nucleotide and derived amino acid sequences of the SsoII restriction endonuclease and methyltransferase."
    Karyagina A.S., Lunin V.G., Degtyarenko K.N., Uvarov V.Y., Nikolskaya I.I.
    Gene 124:13-19(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 47.

Entry informationi

Entry nameiMTS2_SHISO
AccessioniPrimary (citable) accession number: P34879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 7, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Plasmid

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

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 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.