ID A0A1G9C045_9CLOT Unreviewed; 498 AA.
AC A0A1G9C045;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=SAMN04487833_10332 {ECO:0000313|EMBL:SDK45028.1};
OS Sarcina sp. DSM 11001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Sarcina.
OX NCBI_TaxID=1798184 {ECO:0000313|EMBL:SDK45028.1, ECO:0000313|Proteomes:UP000199127};
RN [1] {ECO:0000313|EMBL:SDK45028.1, ECO:0000313|Proteomes:UP000199127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11001 {ECO:0000313|EMBL:SDK45028.1,
RC ECO:0000313|Proteomes:UP000199127};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNFZ01000003; SDK45028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9C045; -.
DR STRING; 1798184.SAMN04487833_10332; -.
DR OrthoDB; 9815272at2; -.
DR Proteomes; UP000199127; Unassembled WGS sequence.
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 CDD; cd02440; AdoMet_MTases; 1.
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; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR Pfam; PF07669; Eco57I; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SDK45028.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199127};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDK45028.1}.
FT DOMAIN 138..236
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 498 AA; 57345 MW; 2D2B5808161C5227 CRC64;
MLEYIINETN KFLEQMPKSK RKKKGQFFTS KETAEFMATM FQLEGLPLEI NILDPGTGTG
ILSAAVVEHL LEADEKRSIH LTCYETDGDV LPVLKNNMVY LLSKAGDRFS YEIREQDYIL
SQQDDFNETF FASEQQTKYD LIIGNPPYLR VMRDNPAALA MPKVVHGAPN LYFLFASMSL
FNLKDNAEMV YIIPRSWTSG AYFKAFRQYF LGEGKLLQIH LFVSRDKVFS SEEVLQETMI
VKVKKTQIVP DEVRITSSQS NSDFNEISEL KVPYSSVVSG RDLYVYLPTS KEDIDIIQRI
NTYQKTLPDE GMRMKTGIVV DFRQWDDLRK EPGDHILPLF YSQHIRNGRV NHQPSGKEFD
WIIDEKPGLI QRNKNYVFCK RFTAKEERRR LQCGVYLPED FKEYEYIGTQ NKINFVDKTD
GSEMDLSTTY GVYALLNSTL FDMYYRILNG STQVNSTEIN SIPVPPAATI ARIGEKVIDS
NDLSTDNCDR ILKEVAYG
//
