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Database: UniProt
Entry: J5JVE0_BEAB2
LinkDB: J5JVE0_BEAB2
Original site: J5JVE0_BEAB2 
ID   J5JVE0_BEAB2            Unreviewed;      1142 AA.
AC   J5JVE0;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=DNA (cytosine-5-)-methyltransferase {ECO:0000256|ARBA:ARBA00011975};
DE            EC=2.1.1.37 {ECO:0000256|ARBA:ARBA00011975};
GN   ORFNames=BBA_04899 {ECO:0000313|EMBL:EJP66406.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP66406.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP66406.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP66406.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
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; JH725160; EJP66406.1; -; Genomic_DNA.
DR   RefSeq; XP_008598218.1; XM_008599996.1.
DR   AlphaFoldDB; J5JVE0; -.
DR   STRING; 655819.J5JVE0; -.
DR   GeneID; 19887911; -.
DR   HOGENOM; CLU_003836_2_0_1; -.
DR   InParanoid; J5JVE0; -.
DR   OrthoDB; 317994at2759; -.
DR   Proteomes; UP000002762; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.490; -; 2.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF54; DNA METHYLTRANSFERASE DIM-2; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01016}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002762};
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}.
FT   DOMAIN          407..524
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          661..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1115..1142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1115..1131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        768
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   1142 AA;  128283 MW;  C9A104A1163C14A4 CRC64;
     MKLTADLDLD LDLNLDLDLD LDLDAISSEQ HDTRILATTC LPGVLSGIDY DGSYSSHGSK
     DDDLEEDGPT GSYPISVHIP ECMLISPRSC YTPFDPPCPV ASERDALRIL LPQRYAKNGF
     LELKLDDFAV YCDTKFRPEE MRSLSQLGTE PHSTPLFFDG MLSHGTQSLY VRRVRIHALP
     IGNYGQESRH QTRDNIWIQS EENATSDVFY KLGSPAPEYK RFFELFVWVA DLAKYFVDFL
     TVMRAIERPV TIHHFRRDFA AWLLALYAKS DKIEAVKTWM CKHPRQDYRS AVNANVDFLH
     KESVGVLGER RAYFHDLWNE VFFFQTYTPY IAHNEDKCTI VTKYIYDCFH HLPFGKRLKV
     VDLSAHTKRL RLEVIAQRPM LPINGTQVTP AGHGKIGPGD TISTARDTVD SGTDWEKEEA
     KGDEYSDLWF ALVQSVSVNS DGVRVFEVIW YYRPVDTLCG LMQYPWSDEL FLSDHCSCEE
     GTKIREDEVR SVHEVDFGGT PETTKEFFCR QSYLSDDKIW VTLTQSHLTC RHNNDAPIPD
     SAEEYCLGDT VLVKSGRNSN VCHPCEIIET KQENGRLRFV FRKLPIRHAV DLTARNAPPN
     EVVYTDEIVK SGPSSIVSRC HVRWFPQTRP VPTPYDRDGV GAFFFLTHQK KWTGNGYITS
     PLEEAPPSLN QGHDPQQDSK PKLRGLDLFC GGGNFGRGLE EGGSVTMKWA NDVNSKALHT
     YMANTEPGQI YPFLGSIDDF QRLAFQGRFA DNIPQVGEVD FISGGSPCPG FSQLTNDKET
     DAQRKNQSLV AAFASCVDLY RPKYGILENV AGIIQKHQNR GHDVFSQLMC ALVGMGYQAR
     LVLLDALSCG SAQVRSRVFI IFAAPGWTLP EAPIQTHSHQ PNVKNFKLGR LPTGEPMARR
     EVASCTPFSY KSASQAAAGL PSLYDATPDI CIAFPDHRVV SHTNTNTMRN RIRLIPKAPY
     GMNFSQAWYG RLGTRPRVAG RGVLTRSERN MFSLRGEATM STSIQSRAYG RQPPNQPMAT
     IVTRASPRDA KQGRTIHWSE DRCLSVMEAK RGQGFLDEEL LLGSADVQYR IIGNSVAREV
     SLALGVVFAE AVMRSYGQGV EDLAVDSEDE VTIKTEMSVP TTPGATRQQG ENNGRNKRRR
     VG
//
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