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P29347

- MTS1_STRSA

UniProt

P29347 - MTS1_STRSA

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Protein

Modification methylase StsI

Gene
stsIM
Organism
Streptococcus sanguinis
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

This methylase recognizes the double-stranded sequence 5'-GGATG-3' in one strand and 3'-CATCC-5' in the other, causes specific methylation on the A of both strands, and protects the DNA from cleavage by the StsI endonuclease. The 2 domains of the protein participates in modification of the two strands.

Catalytic activityi

S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine.

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. site-specific DNA-methyltransferase (adenine-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

Protein family/group databases

REBASEi3512. M.StsI.

Names & Taxonomyi

Protein namesi
Recommended name:
Modification methylase StsI (EC:2.1.1.72)
Short name:
M.StsI
Alternative name(s):
Adenine-specific methyltransferase StsI
Gene namesi
Name:stsIM
OrganismiStreptococcus sanguinis
Taxonomic identifieri1305 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 653653Modification methylase StsIPRO_0000087962Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP29347.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1020.10. 1 hit.
3.40.50.150. 4 hits.
InterProiIPR012186. Ade-mod_methylase_MStsI.
IPR023095. Ade_MeTrfase_dom_2.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR012327. MeTrfase_D12.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF02086. MethyltransfD12. 2 hits.
[Graphical view]
PIRSFiPIRSF036638. M_m6A_StsI. 1 hit.
PRINTSiPR00505. D12N6MTFRASE.
SUPFAMiSSF53335. SSF53335. 3 hits.
TIGRFAMsiTIGR00571. dam. 1 hit.
PROSITEiPS00092. N6_MTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29347-1 [UniParc]FASTAAdd to Basket

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MRYIGSKKLL LPEIKKMVDK HTDGSEEVFL DLFAGTNVVA NYFKQFYTVY    50
SNDMLFFSYV NAKATIENNS KPSFSKLIQA GISSPMTYLQ NLEVNDETIG 100
YYEVAYSPTG EANYLSVHNA KKLDIIRSQI ESWKNQNLLT EHEYYYLLSS 150
LIEALPFISN TTGTYGAFLK HWDKRSLNDL ELQDFTIFDN SKQNKAFNED 200
ANELVQKIKA DIVYIDTPYN SRQYASNYHL LENVARNEHP TLKGITKIFD 250
WKNLKSDYAT KGKALVAMRD LIQNINSTHI ILSYNNEGII SEEDLTNILK 300
EFSVDGIVDI KKIPYRKYQS KNVSKNKEIY ELLFYIQRKP FSKNKTLNKP 350
LNNVRVSSTK KYIKSPLNYI GGKYKLLNQI LPLFPKNINT FVDIFSGGAN 400
VGINVKAKKY IFNDMNTRIN EMFRYFQTQP PVKLVQQIEE KIDEWGLSKT 450
NEDAFLAFRK HYNTNPNPLD LYVLSSFSYN YQFRFNNSME FNNPFGRNRS 500
HFSENMRNNL LNFVTKLQTL DATFTDNYFN EFDFSNLTSN DFIYLDPPYL 550
ITTGSYNDGK RGFSDWNNTS EMKLLNFMDY LNQHGIRFAL SNVTEHKGKT 600
NQLLKDWAYS RNLNVNYLDH NYNNSSHNSK SKGSQEVLIT NYETKTFNLL 650
NTK 653
Length:653
Mass (Da):76,068
Last modified:December 1, 1992 - v1
Checksum:iC4D42B76E5665E91
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D11101 Genomic DNA. Translation: BAA01876.1.
PIRiS35493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D11101 Genomic DNA. Translation: BAA01876.1 .
PIRi S35493.

3D structure databases

ProteinModelPortali P29347.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

REBASEi 3512. M.StsI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.1020.10. 1 hit.
3.40.50.150. 4 hits.
InterProi IPR012186. Ade-mod_methylase_MStsI.
IPR023095. Ade_MeTrfase_dom_2.
IPR002052. DNA_methylase_N6_adenine_CS.
IPR012327. MeTrfase_D12.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF02086. MethyltransfD12. 2 hits.
[Graphical view ]
PIRSFi PIRSF036638. M_m6A_StsI. 1 hit.
PRINTSi PR00505. D12N6MTFRASE.
SUPFAMi SSF53335. SSF53335. 3 hits.
TIGRFAMsi TIGR00571. dam. 1 hit.
PROSITEi PS00092. N6_MTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequence analysis of the StsI restriction-modification gene: presence of homology to FokI restriction-modification enzymes."
    Kita K., Suisha M., Kotani H., Yanase H., Kato N.
    Nucleic Acids Res. 20:4167-4172(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 54.

Entry informationi

Entry nameiMTS1_STRSA
AccessioniPrimary (citable) accession number: P29347
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 11, 2014
This is version 73 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

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