ID H9GDH4_ANOCA Unreviewed; 895 AA.
AC H9GDH4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000007951.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000007951.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000007951.4};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000007951.4}
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; H9GDH4; -.
DR STRING; 28377.ENSACAP00000007951; -.
DR Ensembl; ENSACAT00000008120.4; ENSACAP00000007951.4; ENSACAG00000008029.4.
DR eggNOG; ENOG502QR6U; Eukaryota.
DR GeneTree; ENSGT00940000155459; -.
DR HOGENOM; CLU_006958_9_1_1; -.
DR InParanoid; H9GDH4; -.
DR TreeFam; TF329039; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000008029; Expressed in embryonic post-anal tail 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; IBA:GO_Central.
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:UP000001646};
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 275..333
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 465..597
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..449
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 44..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 693
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 895 AA; 100332 MW; DA8B43D5853B4742 CRC64;
MPSNGPVDTT SSSSVADREA ADARKAETSE APKDTASAPK CPPASAHHSS SSSPMEQVPN
GDVEAGSPEK ATTAAATAEP KGRPRSESEP SALPERETGR TLENGRCCTP KDSPEAPASE
GKEEKEENHY NSLKMEGSRG RLRGGLGCES NLRPRPMPRL TFQAGDPYYI SKRKRDEWLA
RWKRETDNPP ATQLDKAEKK AKVIAGMNAV EEALPRSEPQ KEEEASPPAS QQPTDPASPN
VATTPEPLGP DAADKGMSKT ADDEPEYEDG RGFGIGELVW GKLRGFSWWP GRIVSWWMTG
RSRAAEGTRW VMWFGDGKFS VVCVEKLLPL SSFANAFHQA TYNKQPMYRK AIYEVLQVAS
SRSGKIFPSC PENDETDTSK AVEIQNKQMI EWALGGFQPS GPKGLEPPEE ERNPYKEVYT
EMWVEPEAAA YAPPPPAKKP RKSTAEKPKV KEIIDERTRE RLVYEVRQKC RNIEDICISC
GSLNVTLEHP LFIGGMCQNC KNCFLECAYQ YDDDGYQSYC TICCGGREVL MCGNNNCCRC
FCVECVDLLV GPGAAQAAIK EDPWNCYMCG HKGIYGLLRR RDDWPSRLQM FFANNHDQEF
DPPKVYPPVP AERRKPIRVL SLFDGIATGL LVLKDLGIQV DRYIASEVCE DSITVGMVRH
QGKIMYVGDV RNVTQKHIQE WGPFDLVIGG SPCNDLSIVN PARKGLYEGT GRLFFEFYRL
LHEARPKEGD ERPFFWLFEN VVAMGVSDKR DISRFLESNP VMIDAKEVSA AHRARYFWGN
LPGMNRPLAS TVNDKLELQE CLEHGRIAKF SKVRTITTRS NSIKQGKDQH FPVFMNEKED
ILWCTEMERV FGFPVHYTDV SNMSRLARQR LLGRSWSVPV IRHLFAPLKE YFACV
//
