NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1159/000090817; PubMed=16575165 [NCBI, ExPASy, EBI, Israel, Japan]
Yokomine T., Hata K., Tsudzuki M., Sasaki H.;
"Evolution of the vertebrate DNMT3 gene family: a possible link between existence of DNMT3L and genomic imprinting.";
Cytogenet. Genome Res. 113:75-80(2006).

Comments

FUNCTION: Required for genome wide de novo methylation and is essential for development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. Acts as a transcriptional corepressor for ZNF238. Can actively repress transcription through the recruitment of HDAC activity (By similarity).
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.
SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By similarity).
SIMILARITY: Belongs to the C5-methyltransferase family.
SIMILARITY: Contains 1 ADD-type zinc finger.
SIMILARITY: Contains 1 PWWP 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

AB214886; BAD99023.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001020003.1; -.

UniGene

Gga.6002

3D structure databases

ModBase

Q4W5Z4.

Protein family/group databases

REBASE

11753; M.GgaDnmt3AP.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003886;	Molecular function: DNA (cytosine-5-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001525; C5_DNA_meth.
IPR000313; PWWP.
Graphical view of domain structure.

Pfam

PF00145; DNA_methylase; 1.
PF00855; PWWP; 1.
Pfam graphical view of domain structure.

SMART

SM00293; PWWP; 1.
SMART graphical view of domain structure.

PROSITE

PS00094; C5_MTASE_1; 1.
PS00095; C5_MTASE_2; FALSE_NEG.
PS50812; PWWP; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

421991; -.

KEGG

gga:421991; -.

Phylogenomic databases

HOVERGEN

Q4W5Z4; -.

Other

UniRef

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

Keywords

Cytoplasm; DNA-binding; Metal-binding; Methyltransferase; Nucleus; Repressor; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 877`	`877`	`DNA (cytosine-5)-methyltransferase 3A.`	`PRO_0000313031`
`DOMAIN`	`226 284`	`59`	`PWWP.`
`ZN_FING`	`459 551`	`93`	`ADD-type (By similarity).`
`COMPBIAS`	`448 496`	`49`	`Cys-rich.`
`ACT_SITE`	`675 675`		`By similarity.`

Sequence information

Length: 877 AA [This is the length of the unprocessed precursor]

Molecular weight: 98944 Da [This is the MW of the unprocessed precursor]

CRC64: FC7131DA1D40F84F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVESSDTPKD TAAVPKCPPP CPEASPAEPL PNGDLEADGA QWKGTEEGGA SPKSGRPEED 

        70         80         90        100        110        120 
ETESLADGET GRALENGRCT PKEGLDAPAD EGELAPSDPQ KKRGRRKLLE ATEKSKEEKE 

       130        140        150        160        170        180 
ENNFDSLKME GSRGRLRGGL GWESSLRQRP MQRHTFQAGD PYYISKRKRD EWLARWKREA 

       190        200        210        220        230        240 
EKKAKVIAVM NVVEETPRAE PQKEEEASPP ASQQPTDPAS PNVATTPEPV VADAVDKNTS 

       250        260        270        280        290        300 
KSADDEPEYE DGRGLGIGEL VWGKLRGFSW WPGRIVSWWM TGRSRAAEGT RWVMWFGDGK 

       310        320        330        340        350        360 
FSVVCVEKLL PLSSFSSAFH QATYNKQPMY RKAIYEVLQV ASSRAGKIFP ACPENDETDT 

       370        380        390        400        410        420 
SKVVEIQNKQ MIEWALGGFQ PSGPKGLEPP EEERNPYKEV YTEMWVEPEA AAYAPPPPAK 

       430        440        450        460        470        480 
KPRKSTTEKP KVKEIIDERT RERLVYEVRQ KCRNIEDICI SCGSLNVTLE HPLFIGGMCQ 

       490        500        510        520        530        540 
NCKNCFLECA YQYDDDGYQS YCTICCGGRE VLMCGNNNCC RCFCVECVDL LVGPGAAQAA 

       550        560        570        580        590        600 
IKEDPWNCYM CGHKGVYGLL RRREDWPSRL QMFFANNHDQ EFDPPKVYPP VPAEKRKPIR 

       610        620        630        640        650        660 
VLSLFDGIAT GLLVLKDLGI QVDRYIASEV CEDSITVGMV RHQGKIMYVG DVRNVTQKHI 

       670        680        690        700        710        720 
QEWGPFDLVI GGSPCNDLSI VNPARKGLYE GTGRLFFEFY RLLHEARPKE GDDRPFFWLF 

       730        740        750        760        770        780 
ENVVAMGVSD KRDISRFLES NPVMIDAKEV SAAHRARYFW GNLPGMNRPL ASTVNDKLEL 

       790        800        810        820        830        840 
QECLEHGRIA KFSKVRTITT RSNSIKQGKD QHFPVFMNEK EDILWCTEME RVFGFPVHYT 

       850        860        870 
DVSNMSRLAR QRLLGRSWSV PVIRHLFAPL KEYFACV

Q4W5Z4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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