ID B1VDY7_CORU7 Unreviewed; 607 AA.
AC B1VDY7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=cu0016 {ECO:0000313|EMBL:CAQ03976.1};
OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ03976.1, ECO:0000313|Proteomes:UP000001727};
RN [1] {ECO:0000313|EMBL:CAQ03976.1, ECO:0000313|Proteomes:UP000001727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727};
RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA Puehler A.;
RT "The lifestyle of Corynebacterium urealyticum derived from its complete
RT genome sequence established by pyrosequencing.";
RL J. Biotechnol. 136:11-21(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC Evidence={ECO:0000256|ARBA:ARBA00001279};
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DR EMBL; AM942444; CAQ03976.1; -; Genomic_DNA.
DR RefSeq; WP_012359282.1; NC_010545.1.
DR AlphaFoldDB; B1VDY7; -.
DR STRING; 504474.cu0016; -.
DR REBASE; 17655; CurORF15P.
DR GeneID; 69055500; -.
DR KEGG; cur:cu0016; -.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_031363_0_0_11; -.
DR Proteomes; UP000001727; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR046819; MmeI_hel.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR046820; MmeI_TRD.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841:SF6; DNA METHYLTRANSFERASE A; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF20465; MmeI_hel; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR Pfam; PF20466; MmeI_TRD; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CAQ03976.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001727};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..108
FT /note="MmeI-like helicase spacer"
FT /evidence="ECO:0000259|Pfam:PF20465"
FT DOMAIN 196..450
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 474..591
FT /note="MmeI-like target recognition"
FT /evidence="ECO:0000259|Pfam:PF20466"
FT REGION 9..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 68549 MW; 8CE81B1E3CBAD7FF CRC64;
MAKLFTAMAG DDVDEATGDE APTDPEDEDE ATQRSSMYLT RLLFLLYGDD AGLWEEDLFY
RFVLNHTNAD NLGSQLNSLF EVLNTPENHR RRVPDHFAKF PYVNGSIFAD SLPLEFFDHD
MREALLDACR FHWSRISPAV FGSMFQLVKS KEARRADGEH YTSEKNILKT LEPLFLDELR
DEAKRLIQAK STPGEKPREF RGSLADMVFC DPACGCGNFL VVAYRELRKI ETAVIVAIRE
REGEAGMSLD VSWEQKLSIG QFYGFELNWG PAKIAETAMF LVDHQANLEL ADAIGAAPDR
LPIEITAHIV HDNALALDWS EELPATKGQT FIFGNPPFIG QYSKTKEQTA DMRRAWGADY
DGYLDYLTAW HAMTLRVLSD RAGEFAFVTP NSITQGQPVP ALFRPIQREG WRIKFAHRTF
AWDSEAPGKA AVHCVIVGFT KDRAAKQRLW DYPTPNSDPV PQEVVKGINA YLIDGPNILV
SKSMKPISAE LPLAAQGSKP ADGGNLIIEV DEYETVMADP VAAKYVQPFR MGRELVRGLY
RWCLWLEDLH PADLSKSPVL TERIEACRKF RENSTQSGDA YKRRTTPHLM KISPYRAQLI
HTLEYPV
//
