ID H1VJD2_COLHI Unreviewed; 1246 AA.
AC H1VJD2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN ORFNames=CH063_00349 {ECO:0000313|EMBL:CCF40335.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF40335.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000256|RuleBase:RU000417};
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, ECO:0000256|RuleBase:RU000416}.
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DR EMBL; CACQ02004013; CCF40335.1; -; Genomic_DNA.
DR AlphaFoldDB; H1VJD2; -.
DR STRING; 759273.H1VJD2; -.
DR EnsemblFungi; CCF40335; CCF40335; CH063_00349.
DR VEuPathDB; FungiDB:CH63R_01196; -.
DR eggNOG; ENOG502R6QN; Eukaryota.
DR HOGENOM; CLU_003836_2_0_1; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.490; -; 1.
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 NCBIfam; TIGR00675; dcm; 1.
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 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 434..570
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 1030..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1185..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 800
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 1246 AA; 139110 MW; A14C6D1480D2D233 CRC64;
MVNSTKDLPL GWNPLDLMLS DEEGEDDSVS WELDGDLVEI EHQQTLQALE PPSAPGEEQV
FDEECQAHAV GVVLPSSTLR LSNSLSVDIP ESTLVPPSYL YQGENPVPPP QREWSAVERL
LEEYQWSGVI PRDGYIDIEL DKFVVYTQPY APGQVDYPKA YYPAELRPLQ HLSTKQSNDS
LFFDGVLSVA DCRIHVRQVS FNELPIGKYG IENPTVGSDI WIRSDLNAKR LSRGHKDVCY
RLKNPAKEYK RFHSGFLWIA DLAKHVVDYL EEAHEENRDV SFQDFRSDFS IWLSQKHEGS
LAFSRWRKQY PGTDFGFAVN ANIQFIWKEA NGILSEAARS FRLWKEILHF TAFPSIVASE
STPSTQSDTI PKTVVTPYIC QLFNALPCGV MLEELQPTPK TERLRTETSK ALKLELCTKI
HPAQQPFNMK KPTSGIQVGD VISILPDASI EVSIKRKRVL WNNQDDKLWY GMVQKVHHTR
AGVVFDVTWL YQPNDTPCGQ MTYPWNNEIF FSDHCTCHES PGEGEVIGKI KEEEVLSTHS
VDWDGSQDTE NDFFCRLTYL TAEHCWETFS PAHRRCSFFH QEKEASFEYR LGDTVLVTSS
QEEQAEVVEL TVLPNSNGLA TFRRLPSRQH YESQTPTNEL LYSDEEVSYK VTQIAGRCLV
RIFRPGELIV PPYDRGGAGN AFYITNALQC GRVCPLEDTE FSLRQAFDPS KSFPKLRGAD
LFCGGGNFGR GLEEAGAITM DWCNDMNAKA VHTYVANAGN TVAPFTGPIE ELQKLALLGT
FSDNVPEIGQ VDFVSGGSPC PGFSRLTSDK TKPKQLKNQS LVAAFASFID TYRPKYGLLE
NVEGIVQPET KKKEDVFRQL ICAIVGLGYQ TRCFLLDSWS HGAPQTRTRV FLCFAAPGLK
LPKVPRHSHS HYKARKLKLG QLSNGQFMIE RQLSVPTALK FVSAAAATAD LPDIKDGKPD
FCAEFPDHRV ACGVTKNLRT QMSIIPFHPY AMDFLLSWRD GKGTMTKAER QCFPDRGRRV
NKGSRAFGRV KPSDPMHTIT TKSQPSDSSI GKILHWNQNR PLTVMEARRA QGFRDNDIIL
GNPVDQYQII GNSVSREVSI ALGVSFREAW LGSLVDGEEL DPIVWRPPAQ SMNDAVEDSA
MSPGTPALAE SSRGTPVSKS PRPLPKRKLG SSLGIESFVS KLKKSSRAQM ASEGRVRSNE
QYEPSGSASA LTSTSSSVVT SFSSPAPAST VASVSSRSNV EVVELD
//
