DNM3A_CHICK
ID DNM3A_CHICK Reviewed; 877 AA.
AC Q4W5Z4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA (cytosine-5)-methyltransferase 3A;
DE Short=Dnmt3a;
DE EC=2.1.1.37 {ECO:0000250|UniProtKB:O88508};
DE AltName: Full=Cysteine methyltransferase DNMT3A {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:O88508};
GN Name=DNMT3A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16575165; DOI=10.1159/000090817;
RA Yokomine T., Hata K., Tsudzuki M., Sasaki H.;
RT "Evolution of the vertebrate DNMT3 gene family: a possible link between
RT existence of DNMT3L and genomic imprinting.";
RL Cytogenet. Genome Res. 113:75-80(2006).
CC -!- FUNCTION: Required for genome-wide de novo methylation and is essential
CC for development. DNA methylation is coordinated with methylation of
CC histones. It modifies DNA in a non-processive manner and also
CC methylates non-CpG sites. Acts as a transcriptional corepressor for
CC ZNF238. Can actively repress transcription through the recruitment of
CC HDAC activity. Also has weak auto-methylation activity on some Cys
CC residue in absence of DNA. {ECO:0000250|UniProtKB:O88508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000250|UniProtKB:O88508, ECO:0000255|PROSITE-
CC ProRule:PRU10018};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13682;
CC Evidence={ECO:0000250|UniProtKB:O88508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + S-adenosyl-L-methionine = H(+) + S-
CC adenosyl-L-homocysteine + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:66544, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:82612;
CC Evidence={ECO:0000250|UniProtKB:O88508};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66545;
CC Evidence={ECO:0000250|UniProtKB:O88508};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6K1}.
CC Chromosome {ECO:0000250|UniProtKB:Q9Y6K1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y6K1}. Note=Accumulates in the major satellite
CC repeats at pericentric heterochromatin. {ECO:0000250|UniProtKB:O88508}.
CC -!- DOMAIN: The PWWP domain is essential for targeting to pericentric
CC heterochromatin. {ECO:0000250|UniProtKB:O88508}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; AB214886; BAD99023.1; -; mRNA.
DR RefSeq; NP_001020003.1; NM_001024832.1.
DR AlphaFoldDB; Q4W5Z4; -.
DR SMR; Q4W5Z4; -.
DR STRING; 9031.ENSGALP00000006352; -.
DR REBASE; 11753; M.GgaDnmt3AP.
DR iPTMnet; Q4W5Z4; -.
DR PaxDb; Q4W5Z4; -.
DR GeneID; 421991; -.
DR KEGG; gga:421991; -.
DR CTD; 1788; -.
DR VEuPathDB; HostDB:geneid_421991; -.
DR eggNOG; ENOG502QR6U; Eukaryota.
DR InParanoid; Q4W5Z4; -.
DR OrthoDB; 1015783at2759; -.
DR PhylomeDB; Q4W5Z4; -.
DR PRO; PR:Q4W5Z4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106363; F:protein-cysteine methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR GO; GO:0071774; P:response to fibroblast growth factor; IDA:AgBase.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
DR CDD; cd11729; ADDz_Dnmt3a; 1.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR044108; ADD_DNMT3A.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR040552; DNMT3_ADD.
DR InterPro; IPR030487; DNMT3A.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR23068:SF10; PTHR23068:SF10; 1.
DR Pfam; PF17980; ADD_DNMT3; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Chromosome; Cytoplasm; DNA-binding; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..877
FT /note="DNA (cytosine-5)-methyltransferase 3A"
FT /id="PRO_0000313031"
FT DOMAIN 226..284
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 447..579
FT /note="ADD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT DOMAIN 599..877
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ZN_FING 458..488
FT /note="GATA-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT ZN_FING 499..555
FT /note="PHD-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 675
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
FT BINDING 606..610
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT BINDING 629
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT BINDING 651..653
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT BINDING 856..858
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
SQ SEQUENCE 877 AA; 98944 MW; FC7131DA1D40F84F CRC64;
MVESSDTPKD TAAVPKCPPP CPEASPAEPL PNGDLEADGA QWKGTEEGGA SPKSGRPEED
ETESLADGET GRALENGRCT PKEGLDAPAD EGELAPSDPQ KKRGRRKLLE ATEKSKEEKE
ENNFDSLKME GSRGRLRGGL GWESSLRQRP MQRHTFQAGD PYYISKRKRD EWLARWKREA
EKKAKVIAVM NVVEETPRAE PQKEEEASPP ASQQPTDPAS PNVATTPEPV VADAVDKNTS
KSADDEPEYE DGRGLGIGEL VWGKLRGFSW WPGRIVSWWM TGRSRAAEGT RWVMWFGDGK
FSVVCVEKLL PLSSFSSAFH QATYNKQPMY RKAIYEVLQV ASSRAGKIFP ACPENDETDT
SKVVEIQNKQ MIEWALGGFQ PSGPKGLEPP EEERNPYKEV YTEMWVEPEA AAYAPPPPAK
KPRKSTTEKP KVKEIIDERT RERLVYEVRQ KCRNIEDICI SCGSLNVTLE HPLFIGGMCQ
NCKNCFLECA YQYDDDGYQS YCTICCGGRE VLMCGNNNCC RCFCVECVDL LVGPGAAQAA
IKEDPWNCYM CGHKGVYGLL RRREDWPSRL QMFFANNHDQ EFDPPKVYPP VPAEKRKPIR
VLSLFDGIAT GLLVLKDLGI QVDRYIASEV CEDSITVGMV RHQGKIMYVG DVRNVTQKHI
QEWGPFDLVI GGSPCNDLSI VNPARKGLYE GTGRLFFEFY RLLHEARPKE GDDRPFFWLF
ENVVAMGVSD KRDISRFLES NPVMIDAKEV SAAHRARYFW GNLPGMNRPL ASTVNDKLEL
QECLEHGRIA KFSKVRTITT RSNSIKQGKD QHFPVFMNEK EDILWCTEME RVFGFPVHYT
DVSNMSRLAR QRLLGRSWSV PVIRHLFAPL KEYFACV
