ID I0AKY3_IGNAJ Unreviewed; 1515 AA.
AC I0AKY3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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_1934 {ECO:0000313|EMBL:AFH49640.1};
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:AFH49640.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH49640.1, 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; AFH49640.1; -; Genomic_DNA.
DR RefSeq; WP_014560789.1; NC_017464.1.
DR STRING; 945713.IALB_1934; -.
DR REBASE; 46801; Ial16511ORF1934P.
DR GeneID; 78244811; -.
DR KEGG; ial:IALB_1934; -.
DR PATRIC; fig|945713.3.peg.1939; -.
DR eggNOG; COG0827; Bacteria.
DR eggNOG; COG1002; Bacteria.
DR eggNOG; COG1943; Bacteria.
DR HOGENOM; CLU_002539_1_2_10; -.
DR OrthoDB; 32195at2; -.
DR Proteomes; UP000007394; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0004803; F:transposase activity; IEA:InterPro.
DR GO; GO:0006313; P:DNA transposition; IEA:InterPro.
DR Gene3D; 3.30.70.1290; Transposase IS200-like; 1.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002686; Transposase_17.
DR InterPro; IPR036515; Transposase_17_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; PF01797; Y1_Tnp; 1.
DR SMART; SM01321; Y1_Tnp; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR SUPFAM; SSF143422; Transposase IS200-like; 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:AFH49640.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007394};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 531..697
FT /note="Transposase IS200-like"
FT /evidence="ECO:0000259|SMART:SM01321"
FT REGION 472..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 926..976
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1515 AA; 176771 MW; DF0F5B4711091A38 CRC64;
MKELENLINQ FNGDNLNSLM RAKSRTFRRI DESLPHLNDD QFKDCTLFGE FKINDEYLMV
VITSKVNKPL SERTGKKAQY TLGKKFLKES QRYVGGFFIF YDDKGDFRFS LIYDIPLATG
KRDWSNFRRY TYFVSKDQTN KTFIKQIEEA EFSSLEKIIE AFSVEKVTKQ FYQEIANWYF
WAMDKDKVEF PDDEEKDKEK RNAKNLIRLI TRIIFIWFMK EKNLVPSTLF EKSYIDKIID
YKDKTGSTYY KAILQNLFFA TLNTPMKKDD KKSRIFVEEA IKSGYISDAY LQQGYYRYSR
FIKDKNLFLE LFENIPFLNG GLFESLDKKI DGKEIRVDCF SDNPKNETRL KVPDELFFLD
TEEEIDLSKY LEKGKNKKVT GLLTILKRYN FTIDENTPID QDVALDPELL GKVFENLLAS
YNPETATTAR KATGSYYTPR EIVEYMVNES LIAYLKSSGI LPDSDFSDFN GSREASDTFN
GSREASDTFS GSREASDTFS GSREASGTFF NPYEDVHLFY GKHGKLPHMQ QGSVWYFVTF
RLADSLPKEK VEQLEKEREQ WLKLHEGKKD KLTEEDKKEY YRLFSERVKE WLNSGYGSCV
LKDERIAKIV ADALMHFNHK RYDLDDWVIM PNHVHLLIRP KQNFTLSDIM HSIKSFTAHK
INELLNSKGN VWMHESYDHI VRNEEAFYAI KNYIRRNPEK AKIKLPDVCC SWEKVDESSR
FGDLRSREAS DTFNRSREAS DTFNRSREAS DTFNRSREAS DTLFRKLFDY SYDENPFEDE
ETTLKVIDAI EKIKILDPAC GSGAFPMGVL HKLVLALHKL DPENKIWKQR VLNRVPTEIR
SETEQSLQNK SIDYIRKLGL IENCIYGVDI QEIAIQISKL RFFISLLVEQ QIDDTKPNRD
IRALPNLETK FVAANTLIGL KRPEQMNLVA GEIEELEKKL FEVREEIFYT NSRKEKLALQ
KREKQLREKL KIALKQNGFP NDVAEKITSW DPFDQNTHAD WFDPEWMFGI TSGFDIIIGN
PPYISTKGVD TETKKLFEKF YGFADDTYNH FFFKSFELLK NKGILAFITS KTFWTIQTKK
NLRQLLLNNT LLTLFDTANP FENAMVDTCV AIAQKNKALD AHTVLFLDGK KDLQNPEKFT
IPQADYAHAP NQVFFIPTDF NKKIYQRLGT KVNQLLNQWW DKISTSKNIE KNKKELEQYR
NSLKPGDITL LGLITEGGQG LATANNGKYV GVLEGTKWAD NVLKQRPEKL LLATPFCKEK
NIKTKADAQT FLNNLNEQAI RQLFDNLKEK YGRDIFGQGW LYRIVSKEEI ADVDALSEDE
KLNGIKGTRT FVPYDKGDKD GNRWYAPTPY YIDWSRENVK FLKENSGKKG EGMPVVRNPQ
FYFREGFCWT DVNSTYLKSR LKENGVYDVL TMSLFTSTAY PDWYFVCMIN SKFISEYVGD
FVNSTSHFQI NDARQLPIII PTQEQLKVFE DIFNRAVSVQ KEKFASKISE KEAEEKLEEI
QKELDERVLE MYGVK
//
