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Database: UniProt
Entry: D2H8Z8_AILME
LinkDB: D2H8Z8_AILME
Original site: D2H8Z8_AILME 
ID   D2H8Z8_AILME            Unreviewed;       854 AA.
AC   D2H8Z8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE            EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
DE   Flags: Fragment;
GN   ORFNames=PANDA_006761 {ECO:0000313|EMBL:EFB14890.1};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB14890.1};
RN   [1] {ECO:0000313|EMBL:EFB14890.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
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; GL192588; EFB14890.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2H8Z8; -.
DR   InParanoid; D2H8Z8; -.
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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
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   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          226..284
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   DOMAIN          424..556
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51533"
FT   REGION          1..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..393
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        179..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        652
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
FT   NON_TER         854
FT                   /evidence="ECO:0000313|EMBL:EFB14890.1"
SQ   SEQUENCE   854 AA;  96264 MW;  37DE4420691ACC11 CRC64;
     MKGDTRQLNR EEDASGREDS IITNGGCSDQ SSDSKDAPSP PILEAISTPE IRGRRSSSRL
     SKREVSSLLS YTQVCDGDGE GEDGDSSDTP VMPKLFRETR TRSESPAVRT RNNTSASRRE
     RHRPSPRSTR GRQGRNHVDE SPVEFSATRS LRRRTVSLAG TPWPSPASPY LTIDLTEDDV
     VPQSSSTPYT RLAQDSQQDG FESPQVDAEG RDADSAEYQD GKEFGIGDLV WGKIKGFSWW
     PAMVVSWKAT SKRQAMSGMR WVQWFGDGKF SEVSADKLVA LGLFSQHFNL ATFNKLVSYR
     KALYHALEKA RVRAGKTFPS NPGDSLEDQL KPLLEWAHGG FKPTGIEGLK PNNKQPVVNK
     SKVRRAGSGN LESRKYENKT RRRTADDSAA SDYCPPPKRL KTNCYNNGKD RGEEDQSREQ
     MALDVSNNKS NLEDSCLSCG RKNPVSFHPL FEGGLCQTCR DRFLELFYMY DDDGYQSYCT
     VCCEGRELLL CSNTSCCRCF CVECLEVLVG TGTAADAKLQ EPWSCYMCLP QRCHGVLRRR
     KDWNVRLQAF FTSDTGLEYE APKLYPAIPA ARRRPIRVLS LFDGIATGYL VLKELGIKVE
     KYVASEVCEE SIAVGTVKHE GNIKYVNDVR NITKRNIEEW GPFDLVIGGS PCNDLSNVNP
     ARKGLYEGTG RLFFEFYHLL NYTRPKEGDD RPFFWMFENV VAMKVGDKRD ISRFLECNPV
     MIDAIKVSAA HRARYFWGNL PGMNRPVIAS KNDKLELQDC LEFNRTAKLK KVQTITTKSN
     SIRQGKNQLF PVVMNGKEDV LWCTELERIF GFPVHYTDVS NMGRGARQKL LGRSWSVPVI
     RHLFAPLKDY FACE
//
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