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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
 
 
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