[1]	NUCLEOTIDE SEQUENCE [MRNA]. Chandler V.L., Kaeppler S.M., Kaeppler H.F., Cone K.C.; "Sequences from the plant chromatin consortium."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA]. Bergstrom D., Springer N.M., Schmitt L.T., Guthrie E., Sidorenko L., Selinger D., Kaeppler S.M., Cone K.C.; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: May be involved in the CpXpG methylation and in gene silencing (By similarity).
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
SUBCELLULAR LOCATION: Nucleus (By similarity).
SIMILARITY: Belongs to the C5-methyltransferase family.
SIMILARITY: Contains 1 BAH domain.
SIMILARITY: Contains 1 chromo domain.

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

AY093416; AAM28227.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Zm.599

3D structure databases

HSSP

P83917; 1AP0. [HSSP ENTRY / PDB]

ModBase

Q8LPU5.

Protein family/group databases

REBASE

5016; M.ZmaV.

Organism-specific databases

Gramene

Q8LPU5; -.

Ontologies

GO:0000785;	Cellular component: chromatin (inferred from electronic annotation from InterPro).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from InterPro).
GO:0003682;	Molecular function: chromatin binding (inferred from electronic annotation from InterPro).
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:0006333;	Biological process: chromatin assembly or disassembly (inferred from electronic annotation from InterPro).
GO:0016568;	Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0006306;	Biological process: DNA methylation (inferred from electronic annotation from InterPro).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001025; BAH.
IPR001525; C5_DNA_meth.
IPR000953; Chromodomain.
Graphical view of domain structure.

PANTHER

PTHR10629; C5_DNA_meth; 1.

Pfam

PF01426; BAH; 1.
PF00385; Chromo; 1.
PF00145; DNA_methylase; 2.
Pfam graphical view of domain structure.

PRINTS

PR00105; C5METTRFRASE.

SMART

SM00439; BAH; 1.
SM00298; CHROMO; 1.
SMART graphical view of domain structure.

PROSITE

PS51038; BAH; 1.
PS00094; C5_MTASE_1; 1.
PS00598; CHROMO_1; FALSE_NEG.
PS50013; CHROMO_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8LPU5.

Other

UniRef

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

Keywords

Chromatin regulator; DNA-binding; Methyltransferase; Nucleus; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 915`	`915`	`DNA (cytosine-5)-methyltransferase 3.`	`PRO_0000246696`
`DOMAIN`	`188 313`	`126`	`BAH.`
`DOMAIN`	`445 508`	`64`	`Chromo.`

Sequence information

Length: 915 AA [This is the length of the unprocessed precursor]

Molecular weight: 101611 Da [This is the MW of the unprocessed precursor]

CRC64: D1F4031F729C6A56 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPSSPSSAR PTRASGRKRS AMAEEIHQNQ EEEEEVVAAS TAKRRRKAAS SGKKPKPTPK 

        70         80         90        100        110        120 
QAKPAVAGMK KKGETEKTEP VVDDVCAEEP DEEELAMGEE EAEAEEQAMQ EVVAAVAAGS 

       130        140        150        160        170        180 
PGKKRVGRRS AAASGDHVPE FIGSPVAAAE AHSNWPKRYE RSTAANKPEE DDELKARCHY 

       190        200        210        220        230        240 
RSAKVDNIVY CLGDDVYVKA GENEADYIGR ITEFFEGTDR CHYFTCRWFF RAEDTVINSL 

       250        260        270        280        290        300 
VSINVDGHKH DPRRVFLSEE KNDNVLDCII SKVKIVHVDP NMDPKAKAQL IEHCDLYYDM 

       310        320        330        340        350        360 
SYSVAYSTFA NISSENGQSG SETASGISSD DAGLETSSNM PERTATLLDL YSGCGGMSTG 

       370        380        390        400        410        420 
LCLGAALSGL KLETRWAVDL NSFACQSLKY NHPQTEVRNE KADEFLALLK EWAVLCEKYV 

       430        440        450        460        470        480 
HQDVDSNLAG SEDQEDADTL DKDEFVVQKL IGIRYDGTGR KKGVYFKVQW EGYGPEEDTW 

       490        500        510        520        530        540 
EPIDNLSDCP LKIREFVQEG RKRKILPLPG DVDVICGGPP CQGISGFNRF RNRDEPLKDE 

       550        560        570        580        590        600 
KNKQMVTFMD IVAYLKPKYV LMENVVDILK FADGYLGKYA LSCLVAMKYQ ARLGMMVAGC 

       610        620        630        640        650        660 
YGLPQFRMRV FLWGALSSMV LPKYPLPTYD VVVRGGAPNA FSQCMVAYDE TQRPSLKKAL 

       670        680        690        700        710        720 
LLGDAFSDLP KVENHQPNDV MEYGGSPKTE FQRYIRLGRK DMLDWSFGEE AGPDEGKLLD 

       730        740        750        760        770        780 
HQPLRLNNDD YERVKQIPVK KGANFRDLKG VKVGANNVVE WDPEVERVYL SSGKPLVPDY 

       790        800        810        820        830        840 
AMSFIKGKSL KPFGRLWWDE TVPTVVTRAE PHNQVILHPT QARVLTIREN ARLQGFPDYY 

       850        860        870        880        890        900 
RLFGPIKEKY IQVGNAVAVP VARALGYCLG QAYLGESDGS QPLYQLPASF TSVGRTAVQA 

       910 
NAVSVGTPAG EVVEQ

Q8LPU5 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