ID L5JXA5_PTEAL Unreviewed; 837 AA.
AC L5JXA5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN ORFNames=PAL_GLEAN10024220 {ECO:0000313|EMBL:ELK04089.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK04089.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB031072; ELK04089.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JXA5; -.
DR STRING; 9402.L5JXA5; -.
DR eggNOG; ENOG502QR6U; Eukaryota.
DR InParanoid; L5JXA5; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0010605; P:negative regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR CDD; cd11728; ADDz_Dnmt3b; 1.
DR CDD; cd20155; PWWP_DNMT3B; 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; 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; IPR030488; DNMT3B_ADD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR23068:SF9; DNA (CYTOSINE-5)-METHYLTRANSFERASE 3B; 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; SSF57903; FYVE/PHD zinc finger; 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:UP000010552};
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 228..286
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 407..539
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT REGION 1..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 635
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 837 AA; 94376 MW; 07F024E632F4EF64 CRC64;
MKGDTRQLNR EEDASGREDS IITNGGCSDQ SSDSKDAPSP PILEAISTPE IRGRRSSSRL
SKREVSSLLS YTQDLTGDGD GEGEDGDGSD TPVMPRLFRE TRTRSESPAV RTRNNNSASR
RERHRPSLRS TRGRQGRNHV DESPVEFTVT RSLRRRATSS ASTPWPSPGS PYLTIDLTDD
SVVPQSSSTP YTHLAQDSQQ ESLDSSQVDA EGRDTDGTEY QVPLGRVYCD LVWGKIKGFS
WWPAMVVSWK ATSKRQAMSG MRWVQWFGDG KFSEVSADKL VALGLFSQHF NLATFNKLVS
YRKAMYHALE KARVRAGKTF PSSPGDSLED QLKPMLEWAH GGFKPTGIEG LKPNNKQPES
KTRRRTADDS ATSTDYCPPP KRLKTNCYNN GKDRGEEDQS REQMALDVTN NKSNLEDSCL
SCGRKSPVSF HPLFEGGLCQ TCRDRFLELF YMYDDDGYQS YCTVCCEGRE LLLCSNTSCC
RCFCVECLEV LVGTGTAADA KLQEPWSCYM CLPQRCHGVL RRRKDWNVRL QAFFTSDMGL
EYEAPKLYPA IPAARRRPIR VLSLFDGIAT GYLVLKELGI KVEKYVASEV CEESIAVGTV
KHEGNIKYVN DVRNITKKNI EEWGPFDLVI GGSPCNDLSN VNPARKGLYE GTGRLFFEFY
HLLNYSRPKE GDDRPFFWMF ENVVAMKVGD KRDISRFLEC NPVMIDAIKV SAAHRARYFW
GNLPGMNRPV IASKNDKLEL QDCLEFNRTA KLKKVQTITT KSNSIRQGKN QLFPVVMNGK
EDVLWCTELE RIFGFPVHYT DVSNMGRGAR QKLLGRSWSV PVIRHLFAPL KDYFACE
//
