ID I0AKY1_IGNAJ Unreviewed; 1131 AA.
AC I0AKY1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=IALB_1932 {ECO:0000313|EMBL:AFH49638.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH49638.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH49638.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
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; CP003418; AFH49638.1; -; Genomic_DNA.
DR RefSeq; WP_014560787.1; NC_017464.1.
DR AlphaFoldDB; I0AKY1; -.
DR STRING; 945713.IALB_1932; -.
DR REBASE; 46809; Ial16511ORF1932P.
DR GeneID; 78243562; -.
DR KEGG; ial:IALB_1932; -.
DR PATRIC; fig|945713.3.peg.1937; -.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR HOGENOM; CLU_002539_1_1_10; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000007394; 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; 2.
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 ECO:0000313|EMBL:AFH49638.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007394};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 408..494
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT DOMAIN 665..796
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT COILED 609..636
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1131 AA; 132339 MW; 87695699B01C2005 CRC64;
MDTKQTLENL INQFNSDNLN SLLRAKSRTF RRIDESLLHL NDDQFNNCTL FGEFKVGDED
LMVVITSKVN KPLSERTGKK AQYTFGKKFL KESQRYIGGF FIFYDDKGDF RFSLIYDIPL
STGKRDWSNF RRYTYFVSSS KANKTFRLQF EKADFSDFDK ILKAFSLDAV TDEFYNSFKP
NFDLISASVK GTSNEELKKD FALLFIIRVI FLGFVQKKLW LNKDEDFILN FWKEYKTKYF
GKNLFYNEWV RPLFFESLNN PPGRKVFNRT TPFSENTALA LQMAPYLNGE LFKEKKGYDD
CDLFIPDINI EQFFDFLFSY NFTIEENTLY DQDLELNPEF LGIIFERLVN KEDGAVYTPR
TEVDFMCRIS LVKWLEKNSN VAKKKLYHLF FDKQNENSKE EILNEDEKVH ILSLLKNVTV
CDPAAGSGAF PVGMLQVLDE VIHSLTANDE TNIFERKKEI ISRSLYGVEV KHWAVWINQL
RLWLSLFIDM PDEFKSSFEP LLPNLEFKIR RGDSLVQIIG NKLFTVESHA NISPELKRKI
TELKKEKSDF FFGKSRLNAD LIRKKEADIF KAIIEEQILD KKKTLKVFGK EEANEDIFGS
ISQKEELRLH LDEKKQNEIK EQIKNLEEEL RSIKDEHPLV WNIEFAEIFF DRNGLASQSL
SDGGFDIIIG NPPYVRQEKI SDPNGKFETT EYKELLRQTI YEEFPEHFYL KKDKSKLKIK
IDGKSDLYTF FYLKSLKLLN EKGVHTFICS NSWLDVGYGK WLQEFILENV KLDFVIDNNA
KRSFSSADVN TIITVIEATN QKVNENHKAK FIVYKRPFDE VLNTENLLLV EYAETITKDD
DFRVYPITYK ELKEAGTVYE DEQAKKLGQG IYEGDKWGGK YLRAPDIFFT ILEKGKDKLV
RLGDIAKIKS GIITGDNNFY YRFKETDYDK KKFEVAFKSP KDVTTIMING KDTKYVILKE
NRFLHKRARI LTGDTKNDKF IFHLNSDNIL FEHKFIGIDN YKDEVKLIYI LNSTLIAFIS
EVFGNSNLGE GALYLVPRDI KIFIIPNPDY IDIKYNFIKS FLTRRIKSIF EELGFDKTKP
IRSQNPNPLP DRKALDDIIF DALGLTQAER EEVYYAVAEL VQNRLNKAKS V
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