ID H9H1X7_MELGA Unreviewed; 857 AA.
AC H9H1X7;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN Name=DNMT3A {ECO:0000313|Ensembl:ENSMGAP00000014894.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000014894.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000014894.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000014894.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01016}.
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DR AlphaFoldDB; H9H1X7; -.
DR STRING; 9103.ENSMGAP00000014894; -.
DR Ensembl; ENSMGAT00000015835.3; ENSMGAP00000014894.3; ENSMGAG00000014078.3.
DR GeneTree; ENSGT00940000155459; -.
DR HOGENOM; CLU_006958_9_1_1; -.
DR InParanoid; H9H1X7; -.
DR TreeFam; TF329039; -.
DR Proteomes; UP000001645; Chromosome 2.
DR Bgee; ENSMGAG00000014078; Expressed in hindlimb stylopod and 17 other cell types or tissues.
DR GO; GO:1902494; C:catalytic complex; IEA:Ensembl.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106363; F:protein-cysteine methyltransferase activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0141068; P:autosome genomic imprinting; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:1903926; P:cellular response to bisphenol A; IEA:Ensembl.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043045; P:post-fertilization epigenetic regulation of gene expression; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd11729; ADDz_Dnmt3a; 1.
DR CDD; cd20154; PWWP_DNMT3A; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.10.720.50; PWWP, helical domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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_GATA1-like.
DR InterPro; IPR049554; DNMT3_ADD_PHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR23068:SF10; DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A; 1.
DR PANTHER; PTHR23068; DNA CYTOSINE-5- -METHYLTRANSFERASE 3-RELATED; 1.
DR Pfam; PF17980; ADD_DNMT3; 1.
DR Pfam; PF21255; ADDz_Dnmt3b; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01016};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01016}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 237..295
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 427..559
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 655
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 857 AA; 96678 MW; 0A8ED990CA79463A CRC64;
TPMRKAGRPG RKRKHAQVSS GAQWDSHPQS SLSLTLPSKA SPAEPLPNGD LETDGAQWKG
TEEGGTSPKS GRPEEDETES LADGETGRAL ENGRCTPKEG LDAPANEGEL GSRGRLRGGL
GWESSLRQRP MQRHTFQAGD PYYISKRKRD EWLARWKREA EKKAKVIAVM NVVEETPRAE
PQKEEEASPP ASQQPTDPAS PNVATTPEPV VADAVDKNTS KSADDEPEYE DGRGFGIGEL
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
//
