ID   DMT5_VERDV              Reviewed;        2360 AA.
AC   G2WR64;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=DNA (cytosine-5-)-methyltransferase DMT5 {ECO:0000305};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:J9VI03};
GN   Name=DMT5 {ECO:0000305}; Synonyms=DNMT5 {ECO:0000303|PubMed:33941240};
GN   ORFNames=VDAG_00047 {ECO:0000312|EMBL:EGY13365.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000312|Proteomes:UP000001611};
RN   [1] {ECO:0000312|Proteomes:UP000001611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC   {ECO:0000312|Proteomes:UP000001611};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=JR2 {ECO:0000269|PubMed:33941240};
RX   PubMed=33941240; DOI=10.1186/s13072-021-00396-6;
RA   Kramer H.M., Cook D.E., van den Berg G.C.M., Seidl M.F., Thomma B.P.H.J.;
RT   "Three putative DNA methyltransferases of Verticillium dahliae
RT   differentially contribute to DNA methylation that is dispensable for
RT   growth, development and virulence.";
RL   Epigenetics Chromatin 14:21-21(2021).
CC   -!- FUNCTION: May play a role in cytosine methylation at palindromic 5'-CG-
CC       3' and 5'-C[ACT]G-3' sites in DNA. {ECO:0000269|PubMed:33941240}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + ATP + H2O + S-adenosyl-L-
CC         methionine = a 5-methyl-2'-deoxycytidine in DNA + ADP + 2 H(+) +
CC         phosphate + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:68984,
CC         Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452,
CC         ChEBI:CHEBI:85454, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:J9VI03};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68985;
CC         Evidence={ECO:0000250|UniProtKB:J9VI03};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:33941240}. Chromosome
CC       {ECO:0000305|PubMed:33941240}.
CC   -!- DISRUPTION PHENOTYPE: Very mildly decreases methylation of the fifth
CC       carbon of cytosine (5mC) in DNA (PubMed:33941240). No apparent cell
CC       population growth phenotype, sexual reproduction phenotype, virulence
CC       phenotype, or sensitivity to osmotic, oxidative or genotoxic stress
CC       (PubMed:33941240). {ECO:0000269|PubMed:33941240}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM-
CC       binding methyltransferase superfamily. C5-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01016}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the SNF2/RAD54
CC       helicase family. {ECO:0000305}.
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DR   EMBL; DS572695; EGY13365.1; -; Genomic_DNA.
DR   RefSeq; XP_009649719.1; XM_009651424.1.
DR   STRING; 27337.EGY13365; -.
DR   EnsemblFungi; EGY13365; EGY13365; VDAG_00047.
DR   GeneID; 20701510; -.
DR   KEGG; vda:VDAG_00047; -.
DR   eggNOG; KOG0298; Eukaryota.
DR   eggNOG; KOG4439; Eukaryota.
DR   HOGENOM; CLU_000796_0_0_1; -.
DR   InParanoid; G2WR64; -.
DR   OMA; SMIPYIT; -.
DR   Proteomes; UP000001611; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chromosome; DNA-binding; Hydrolase; Metal-binding;
KW   Methyltransferase; Nucleotide-binding; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..2360
FT                   /note="DNA (cytosine-5-)-methyltransferase DMT5"
FT                   /id="PRO_0000454227"
FT   DOMAIN          48..507
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   DOMAIN          1258..1575
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          2102..2267
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         2018..2070
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1451..1498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1476..1498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   BINDING         1271..1278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   2360 AA;  264272 MW;  F83105AF9129B81D CRC64;
     MAQKPQQFDV LGDTGARVDR PRDSLALIFK RALELGLDDV SQDGGVRFTV GTMCSGTDAP
     ILALRELQDA ALAMGYNHLF DFDHQFSVEI EAYKQAFIER NSKPSGEIYR DVIQVSDPSR
     KDAITAHGSL APIPAAPDLL VAGSSCVDFS KLNNKRDILA KHSVLSRLYE EAKNTKNGLD
     FGTVTPQSQS HDVRMALQDV RDSFHTEGES VKTFGSILQF IYDQRPKLII LENVSHAPWR
     AFTHFWLPLV GYVALSMKVD SKNFLVPQTR TRGYLVAVDQ WHYGTELSTR MARLWSSMME
     SSNWFPNQYP EVHKFLLSSM DQRILEARAI EERKIAENMT RDVEARMCAY DHAKVRRQQG
     LGPDRPFTQR DGRGNLLPRD TSWQAYIRGT SSRVQDLLDI TWLSERKKGG RDLNYKAKYL
     DLGEGVERLK TQIGIVGCVL PDGDLFATDQ GRPILGVEAL SLQGLPIDRI RTSVETQADL
     HDMAGNAMTT TVVGAATLCI LIAERQVTRS SGFHDGLPLL DNGASTRTQH LKHLFAIRQS
     DRNGAADGAF ALLQHCPSYS TAQKDQAAVA HLIMIHQKGR RYCPCAGYRK HNPATGLMIC
     TLCNQVRCVT CAGNPAHAFE TLLTGPLWSW DETIHALRGI LPNRFALTGG HGIPQDDKDV
     KSLCSSLYTT EKENGNITTR LRELRKCLGA VYYLDHFDNS QVIVATYVST CGRIELSIGL
     DQVVWYLYLP EPLEPGSFNQ QPAPPIARAI LDKSADNVFP SCLSWEIFFL QPVPVVLSLE
     PQSDSTFRCF VTEFNGQPIK SYPIIPMAAT ELMVGVEGVY EFSQTCGTPF DLLYSRRTAG
     SEPSSAPCYL FLDTKHTTEP EEDSWVMSQS VSKLEPGTHR EVLCKFSSSW KEQEQKLRQH
     GTPQTVQCEI PGLWRSVHQT NGALMNISMS DVHLAPDRMT AETSEDLHVI IPGALNFPDV
     AQAPIPVLQL RIDIPDLPFP VHLLPQLWKT DGEIFKECAK ETDSGEKWMR VSDHHHKDAL
     SLISFALGAL KANHLPREFT VGILERAGAV CQSLDADFPN PKVHLLWEGF KVKKLFDDSE
     AAQQLAESYS KRPLPLELDV QIVRADQPRH TGDLYSGRAG GNIAQEPELI IRILFNPTAL
     AHRAWLHIPR DGLIRGIRRD VMQDGHIGFA VDVEFVDPSL KMIEPFEACL SQDVISSATY
     ASAIQLPSFD SCGVQLRPDQ IQSVQWMIEK ESSNSCFVER EVEEFLVPSS SIRLRSHAEV
     VNRARGGVLA HDVGFGKTIA TLALIDHQRN QSNERSVTER YAWTQERHCH LKATLIVCPP
     QIVDQWRDEI ERFLGSENWN VVVINAKTPF HRGILEMADI VILSTAFIHS TAFVQALTRV
     AGAANFHDAS SASSREFNIW YREAVTDLED SCQCYADNNR NNGALAKHIS LRTQERKASF
     EKARAACIVE SRRKDQKSKA TARTQRAKKK SKKPRRTAAA AAESDHSAES DSDSAMDDRK
     RKVATSHVVS DFKDATVLQM YSFDRVVLDE FSYENKSTAA FVANCVASSK WILSGTPPMA
     DLSQVCAIAD LVNMHVARPE ASVPRSFPSI TRGPRLDKTT RGEAMRQYAD PKSAQFALER
     HEQARTFLEH KMTRRETDIS HIGVTEQVVV CRLDPVSSVV YAQLQQVLYD ARWDIEEVPG
     DMRAIIDWLL QQTGNNKASK ARENLRMSWH NTIQSLLVQS STNLSAYGEN MKKLGMDVRA
     GAVSGITVLT SMRTIYQRLQ ARSKAMIKSQ FDMLMYVVDQ VQMSGLLTMT NAKGRDKTKQ
     DKAMYYQDHL DDFIQRFTAA RPWSFGDAEI RDDFWKGGNG VYGAIDWWKL TEEDVEAMDE
     DELKHVETKL VCFKASYNPE SQMEATGQQL EESVCDLLNA NVLDQYHEAE PEKVAANIGL
     ASATLLDVYW KDTAKSKDFE FGNKFRPYRP KLNEEETDRG TSHDQATNRM AMALQSVQAG
     IEEYIRQARR LRVLGIVQDL FAFAQALEAG HQPNAPTCSV CGSQDNTEMK DLSLFITCGH
     LLCSGCVAAH EHQHGQAEST TGEVLCPVDS CSAMARSALV PCTQLISATA ASTLDFEGKS
     AKVMKILDVI RTDVKDDEKV LLFVSNKKLK AQLSDALEED DNVDVYMTTG THHDTDAIRS
     FKEPNEDGRK KVLVQSLMSE ESAGTNLTEA NHVMFAAPLH TDRRNHYMYM RQARGRAIRF
     GQTRPVRVYH FVTAHTMEVD VLEHRLGHKL LIPEGGDRMP LDDLDYKLYA LDTRAASRGP
     PSATKEASAA PTISSTLRRI RPYIDEVETR KLLDSQEYDE WQDRLDVSPS AATKQTPWFR
     SQVVEQSADE VYDDDVEVGN