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Database: UniProt
Entry: W5NHN0_LEPOC
LinkDB: W5NHN0_LEPOC
Original site: W5NHN0_LEPOC 
ID   W5NHN0_LEPOC            Unreviewed;       948 AA.
AC   W5NHN0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE            EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020139.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000020139.1}
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   EMBL; AHAT01015721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01015722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01015723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01015724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01015725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01015726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015204072.1; XM_015348586.1.
DR   AlphaFoldDB; W5NHN0; -.
DR   STRING; 7918.ENSLOCP00000020139; -.
DR   Ensembl; ENSLOCT00000020172.1; ENSLOCP00000020139.1; ENSLOCG00000016317.1.
DR   GeneID; 102694135; -.
DR   CTD; 553189; -.
DR   eggNOG; ENOG502QR6U; Eukaryota.
DR   GeneTree; ENSGT00940000155459; -.
DR   InParanoid; W5NHN0; -.
DR   OMA; PRCFCVE; -.
DR   OrthoDB; 2904336at2759; -.
DR   Proteomes; UP000018468; Linkage group LG1.
DR   Bgee; ENSLOCG00000016317; Expressed in larva and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032776; P:DNA methylation on cytosine; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
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:UP000018468};
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          328..386
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   DOMAIN          518..650
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51533"
FT   REGION          1..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        746
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   948 AA;  107438 MW;  B3639A9F9482E3C9 CRC64;
     MPSNATATTT TFKSSDFDYD AAANKMSEDQ EQDRGKEPGN SVPLRKVGRP GRKRKQLPVN
     SCETSKEDVG SKCHASVESQ SSEQVHNGDV DSHPGDTIAA SSKQGRNIPE NGVPRESVRR
     SEELPDQEAQ GQGYRKGRPD SSLENGFSTP PDDQDSEKDG EQVPPTPRKK RGRRKLEHPE
     KHTEEQDESS CETVKTEQGT RARLRGGLGW ETSLRQRPMQ RITFQAGDPY YISKRKRDEW
     LAKWKMEAEK RAKLVAVMNA MEEPAGNEAQ KEEEEVVVNQ LPPQQHTDPA SPTVATTPEP
     VSAETVDKSI PKSTDVEPEY EDGRGFGIGE LVWGKLRGFS WWPGRIVSWW MTGRSRAAEG
     TRWVMWFGDG KFSVVCVEKL MPLSSFSNAF HQPTYNKQPM YKKAIYEVLQ VASSRAGKIF
     PTCPDTDETD TSKSVDLQNK QMIEWAMGGF QPTGPKGLEP PEEERNPYKE VYTEMWVEPE
     AAAYTPPPPA KKPRKSTAEK PKIKEIIDER TRERLVYEVR QKCRNIEDIC ISCGSLNVSL
     EHPLFLGGMC QNCKNCFLEC AYQYDDDGYQ SYCTICCGGR EVLMCGNNNC CRCFCVECVD
     LLVGPGAAQA AIKEDPWNCY MCGTKGIYGL LKRREDWPSR LQHFFANNHD QDFDPPKLYP
     PVSAEKRKPI RVLSLFDGIA TGLLVLKDLG IQVERYIASE VCEDSITVGI VRHQGRIMYV
     GDVRNVTRKH IQEWGPFDLV IGGSPCNDLS IVNPARKGLY EGTGRLFFEF YRLLHEARPK
     EGDDRPFFWL FENVVAMGVS DKRDISRFLE CNPVMIDAKE VSAAHRARYF WGNLPGMNRP
     LAAMTNDKLD LQDCLEHGRT AKFSKVRTIT TRSNSIKQGK DQHFPVYMNE KEDILWCTEM
     ERVFGFPVHY TDVSNMSRLA RQRLLGRSWS VPVIRHLFAP LKEYFACL
//
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