NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
DOI=10.1093/nar/20.8.1891; PubMed=1579490 [NCBI, ExPASy, EBI, Israel, Japan]
Rafferty J.A., Elder R.H., Watson A.J., Cawkwell L., Potter P.M., Margison G.P.;
"Isolation and partial characterisation of a Chinese hamster O6-alkylguanine-DNA alkyltransferase cDNA.";
Nucleic Acids Res. 20:1891-1895(1992).

Comments

FUNCTION: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine.
COFACTOR: Binds 1 zinc ion (By similarity).
SUBCELLULAR LOCATION: Nucleus (Probable).
SIMILARITY: Belongs to the MGMT 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

X65081; CAA46209.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P16455; 1QNT. [HSSP ENTRY / PDB]

SMR

P26186; 6-178.

ModBase

P26186.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003908;	Molecular function: methylated-DNA-[protein]-cysteine S-methyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006281;	Biological process: DNA repair (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001497; MethylDNA_cys_MeTrfase_AS.
IPR014048; MethylDNA_cys_MeTrfase_DNA_bd.
IPR008332; MethylG_MeTrfase.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.

PANTHER

PTHR10815; MethylDNA_cys_mtrans_DNA_bd; 1.

Pfam

PF01035; DNA_binding_1; 1.
PF02870; Methyltransf_1N; 1.
Pfam graphical view of domain structure.

TIGR00589; ogt; 1.

PS00374; MGMT; 1.

Phylogenomic databases

HOVERGEN

P26186; -.

Other

UniRef

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

Keywords

DNA damage; DNA repair; DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Transferase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 209`	`209`	`Methylated-DNA--protein-cysteine methyltransferase.`	`PRO_0000139358`
`ACT_SITE`	`149 149`		`Nucleophile; methyl group acceptor (By similarity).`
`METAL`	`5 5`		`Zinc (By similarity).`
`METAL`	`24 24`		`Zinc (By similarity).`
`METAL`	`29 29`		`Zinc (By similarity).`
`METAL`	`89 89`		`Zinc (By similarity).`
`BINDING`	`99 99`		`DNA; via amide nitrogen (By similarity).`
`BINDING`	`118 118`		`DNA (By similarity).`
`BINDING`	`119 119`		`DNA; via amide nitrogen (By similarity).`
`BINDING`	`127 127`		`DNA (By similarity).`
`BINDING`	`132 132`		`DNA (By similarity).`
`BINDING`	`155 155`		`DNA; via amide nitrogen (By similarity).`
`MOD_RES`	`10 10`		`Phosphothreonine (By similarity).`
`MOD_RES`	`205 205`		`Phosphoserine (By similarity).`

Sequence information

Length: 209 AA [This is the length of the unprocessed precursor]

Molecular weight: 22333 Da [This is the MW of the unprocessed precursor]

CRC64: 38CD50618BAB8A8D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAETCKMKYT VFHSPLGKIE LCGCERGLHG IRFLSGKTPS SDPKEAPASP ELLGGPEDLP 

        70         80         90        100        110        120 
ESLVQCTTWL EAYFQEPAAT EGLPLPALHH PVFQQDSFTR QVLWKLLKVV KFGEMVSYQQ 

       130        140        150        160        170        180 
LAALAGNPKA ARAVGGAMRN NPVPILIPCH RVICSNGSIG NYSGGGQAVK EWLLAHEGIP 

       190        200 
TRQPACKDLG LTGTRLKPSG GSTSSKLSG

P26186 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