ID A0A1S3MG33_SALSA Unreviewed; 1511 AA.
AC A0A1S3MG33;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN Name=LOC106572465 {ECO:0000313|RefSeq:XP_014002152.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014002152.1};
RN [1] {ECO:0000313|RefSeq:XP_014002152.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014002152.1};
RG RefSeq;
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 RefSeq; XP_014002152.1; XM_014146677.1.
DR GeneID; 106572465; -.
DR OrthoDB; 2904336at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
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 Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 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; IPR001525; C5_MeTfrase.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
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:SF54; DNA (CYTOSINE-5-)-METHYLTRANSFERASE; 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; PF00307; CH; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 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; PS50021; CH; 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:UP000087266};
KW S-adenosyl-L-methionine {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 17..119
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 918..974
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1081..1213
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT REGION 156..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1511 AA; 168655 MW; F20187E9B402CC26 CRC64;
MATNVDLDQT PDATAEKCSR FELLDWLNKT LDIKFTEVEQ ICSGSCYCQL MDWIFPGCID
LSTVKFQAQD MSDFLHNYNM LQAGFNKTGV TKPVPVEELI NGKFQPNFIF LKWFKSFFQA
NLKGQVYNPV EARQGQDIQP ARFRFRSPQR LHLEDCNSAS RSPSQSGGLE TNTDEEALGK
YQRKRIIYED IWRETYSWVG ASTLGEIYAY CSLCDLNFNI YHSGLFDLKR HSQSKKHSKL
SLAASDVTLT PDSGKSRQGS CSDLPPCSEL VFRFIQANCV SGPSAAEDQV STRYGQYVLG
LQYPEDIVSA CQKTPYCIYM YGGVVLGQTD MASVVLVGYF DEKAARHCIR LLDVLQPPDD
GNAGEKTAAA LVETLERFGL PAANLAALYS DGNGSASEPI CSQLRELNPN IVVLSGLYGV
ADAACHAGVS ELSTQAQELI VDIYSHYSSC STKDDNLKEL FSSISGTDGL TLPLTTCCLN
FCMLVRKVLG MWTDLISHFS SCNKEDNIDN KAKLICTQLQ DPKLRAIFMF LDQALEPLRV
FQERLHHHEG SARADLVQIL QDASGLLRSY ASSFLRPQAV VDFLKERDTF LLKTTKFHLA
GAELNVGGAV VEDFLCELSE TGSEALKLLQ EQALSFYTAL TASVAEGLPL SDGVLRSMAQ
LLSPQGRLKV TGKAVGELGA KLGLCSSPEE ISQLNKEFLE YQLAEEGEGD EGENRCDGGV
QNDSAAPSLE QHWSTVLKAS GSTTIFRKLV LTLLAMPCPP LEAQKVFTQA VENGDAAQFA
DSVTESELDS IQEVDLTSDS TLSDNNSVNG LGRKKKNRGR SRKIPSGSLL IMEASMCCFP
EGNYLNGTVK PCTVRLQKII NGPKNEDNTV FVEDDVIWTN TMEPLKNANQ TSASNVSPPS
RRAAKKGVDY QDGKGFPTGE LVWGKVKCFS WWPGLVVLWK SNKTPPVSMR RVEWFGDSMF
SEICTERLLH FAAFAKCFCK NSYASFPTYK DAIYQVLELA GERCEKFFLA AGNKQEELKL
MLDWAHSGFQ PTGPDGFNPP AADLMAESSD SDYQPPSKKK YVNKKRPSSG NLVYSRGAMV
QKVMKGKKIE EFCLSCGTPQ IHTFHPLFEG SLCQKCKENF IETLYRYDED GYQSYCTVCC
SGQEVILCGN ASCCRCFCKD CLNFLVGDGT FNQLKDVDPW SCFMCLPSQC NGSLKLRPDW
SVRVQEFFVN NSALEFEPHR MYPSIPAHQR RPIRVLSLFD GIATGYLVLK DLGFIIKRYI
ASEICGDSIA VGMIKHQGQI EHINDVRTIT RKHLAEWGPF DLLIGGSPCN DLACVNPARK
GLFEGTGRLF FEYYRMLTMM RPREDDDRPF FWLFENVVAM SGHDKADICR FLECNPILID
AVKVSPAHRA RYFWGNLPGM NRPLATSLDD KVNLQDCLEL GRTAKYNKIR TITTKSNSIR
QGKMGPLPVD FNGKEDYLWC TEMEKIFGFP KHYTDVNNMG RSQRQKVLGR SWSVPVIRHL
FAPLKDYFAC E
//
