[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DSM 3848 / THF; PubMed=1512204 [NCBI, ExPASy, EBI, Israel, Japan] Noelling J., de Vos W.M.; "Characterization of the archaeal, plasmid-encoded type II restriction-modification system MthTI from Methanobacterium thermoformicicum THF: homology to the bacterial NgoPII system from Neisseria gonorrhoeae."; J. Bacteriol. 174:5719-5726(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DSM 3848 / THF; DOI=10.1093/nar/20.24.6501; PubMed=1336177 [NCBI, ExPASy, EBI, Israel, Japan] Noelling J., van Eeden F.J.M., Eggen R.I.L., de Vos W.M.; "Modular organization of related Archaeal plasmids encoding different restriction-modification systems in Methanobacterium thermoformicicum."; Nucleic Acids Res. 20:6501-6507(1992).

Comments

FUNCTION: This methylase recognizes the double-stranded sequence GGCC, causes specific methylation on C-3 on both strands, and protects the DNA from cleavage by the MthTI endonuclease.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
SIMILARITY: Belongs to the C5-methyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M97222; AAA73370.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X68366; CAA48436.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B42941; B42941.

RefSeq

NP_039765.1; -.

3D structure databases

HSSP

P20589; 1DCT. [HSSP ENTRY / PDB]

ModBase

P29567.

Protein family/group databases

REBASE

3448; M.MthTI.

Ontologies

GO:0003886;	Molecular function: DNA (cytosine-5-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0006306;	Biological process: DNA methylation (inferred from electronic annotation from InterPro).
GO:0009307;	Biological process: DNA restriction-modification system (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001525; C5_DNA_meth.
Graphical view of domain structure.

PANTHER

PTHR10629; C5_DNA_meth; 1.

Pfam

PF00145; DNA_methylase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00105; C5METTRFRASE.

TIGRFAMs

TIGR00675; dcm; 1.

PROSITE

PS00094; C5_MTASE_1; FALSE_NEG.
PS00095; C5_MTASE_2; 1.

Genome annotation databases

GeneID

2193586; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Methyltransferase; Plasmid; Restriction system; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 330`	`330`	`Modification methylase MthTI.`	`PRO_0000087894`
`ACT_SITE`	`73 73`		`By similarity.`

Sequence information

Length: 330 AA [This is the length of the unprocessed precursor]

Molecular weight: 37360 Da [This is the MW of the unprocessed precursor]

CRC64: EFC15E57D86385A5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNMDIASFFS GAGGLDLGFT KAGFNIVFAN DNWKGCWKTF EKNHGIKINK KPIEWLKPSE 

        70         80         90        100        110        120 
IPDVVGFIGG PPCQSWSLAG SMCGADDPRG KTFYAYVDLV KEKDPLFFLA ENVPGIVSRT 

       130        140        150        160        170        180 
HLPEFKRLVN SFIDIGYNVE YKVLNAKDYG VPQDRKRVFI VGYREDLNLK FEFPKPLNKK 

       190        200        210        220        230        240 
VTLRDAIGDL PEPKPALEKN RSNGENLEVP NHEYMTGTFS SRYMSRNRVR SWDEVSFTIQ 

       250        260        270        280        290        300 
AGGRHAPCHP QANKMIKVGP DKFIFDPESP KPYRRLSVRE CARIQGFPDD FIFYYKNVAD 

       310        320        330 
GYTMVGNAVP VKLAEELAKK IKKDLEGVLN

P29567 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools