ID B0VHW4_CLOAI Unreviewed; 1099 AA.
AC B0VHW4;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=CLOAM1063 {ECO:0000313|EMBL:CAO80935.1};
OS Cloacimonas acidaminovorans (strain Evry).
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO80935.1, ECO:0000313|Proteomes:UP000002019};
RN [1] {ECO:0000313|EMBL:CAO80935.1, ECO:0000313|Proteomes:UP000002019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX PubMed=18245282; DOI=10.1128/JB.01248-07;
RA Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA Weissenbach J., Le Paslier D.;
RT "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT provides a first glimpse of a new bacterial division.";
RL J. Bacteriol. 190:2572-2579(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};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; CU466930; CAO80935.1; -; Genomic_DNA.
DR RefSeq; WP_015424793.1; NC_020449.1.
DR AlphaFoldDB; B0VHW4; -.
DR STRING; 459349.CLOAM1063; -.
DR REBASE; 20293; CacGORF1063P.
DR KEGG; caci:CLOAM1063; -.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_002539_1_1_0; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000002019; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000002019};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 411..494
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 669..792
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT COILED 580..607
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1099 AA; 128431 MW; C38FD01FBD68D95E CRC64;
MELKPYLVLP SNFSLDNWIS YFDKASSVFA EKIDHLPKLN DVNFSEITAL GNLSFSDATN
CGIYLIKVNR PLTDKTARKK QFDKAIEIIK QKQIQAGLFI FYDENKSFRF SFIYPVYKGT
KRAYSNYRRH SFYINADLPN KTYQLQLSKY KLDSLVEIKE MFSVERISDL FYQEFEQEYA
KLQKGIKHLY NQDITAEKRG DFSLPFVLRI IFLGFVQKKG WLGNNSKFIQ NYIKTYNSDI
HKNGIYQDLL CPLFFQALNS APSQKNKFSF PNITEPFNTQ LVNAPYLNGG LFRKHENYDL
DALYITDEAI NNFTEFLFSY NFTLEENTLY DEELELNPEF LGIIFEKLIN KQYGAIYTPR
LEVDFMCRIS LVKYLQKNCS SSIKLEELYK LFFPEYGDEN EQTAGNFSFE EAKEILEKLE
QITICDPAIG SGAFAVGMLS VLDEIECLLY EKFLHQETPS NPFERKKRII FQSLYGVEVK
QWAVWITQLR LWITLLIDAE DNLKNSEEPL LPSFDFKIRQ GDSLIQILGN YLFPISGEGL
VGLDIQRKIK ELIKLKTDYY YNKCSNKQFE IEKKQQDLYL DILLKKRNEL NAALKRLERD
SINEVQDNFL DSDIQIELDL STKKQKHEIE KLKYQINIVE YEIKQIMNHN LPFIWIIDFP
EIFIENRGFD IVIGNPPYVP QEEIEDPLNK IERSKYKALL KTMVAQDFPQ DLQESNINGK
SDLYTFFYIR GLRLLNPKGI LTFISSNSWL DVEFGAWLQK FLLENCPVYF IIDNLSKRVF
RSADINTIIA VIGAKQKMVA SDDLIRFAAF KLPFESSLYT ENFLTIEETQ NRIDYDDLRV
NPVPRIKLLE EGLNNSRDNK YIGNMWGSYY IRSPHFFLNI LEKCENKLVN LNKVAVIKGY
IHDNSVSDKY PTKYFVKSVK DINVLGVDTN TPGVIRKGIK STNGNDIIAP ILYPRTFGSR
HIVIRNLSNV FFKEFYKIIP IEEENVDSIF IQLNSSFGVF QRELIGLSNL GGGALKFSIN
SIGLFRFFTK IEYKDYCDIL EPLLTEKVDD FFVECNKSYR IELDDIIFNY LGLTKDERRI
FMDILKDMIE NRLNRASSC
//
