ID A0A1N6Y3W0_9SPIO Unreviewed; 582 AA.
AC A0A1N6Y3W0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN05920897_1383 {ECO:0000313|EMBL:SIR09260.1};
OS Alkalispirochaeta americana.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Alkalispirochaeta.
OX NCBI_TaxID=159291 {ECO:0000313|EMBL:SIR09260.1, ECO:0000313|Proteomes:UP000186400};
RN [1] {ECO:0000313|EMBL:SIR09260.1, ECO:0000313|Proteomes:UP000186400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASpG1 {ECO:0000313|EMBL:SIR09260.1,
RC ECO:0000313|Proteomes:UP000186400};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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};
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DR EMBL; FTMS01000038; SIR09260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6Y3W0; -.
DR STRING; 159291.SAMN05920897_1383; -.
DR Proteomes; UP000186400; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SIR09260.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186400};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..157
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 330..397
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 472..506
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 582 AA; 66695 MW; 20AFE3F7F738726F CRC64;
MFVQHMLAVL KSDGRLATVM PHGVMFRGGE EAEARKYFMD HGYLEAIIGL PASLFYGTGI
PACILVLNKK DANKRKNGHV LFINADRGYR EGSARNYLRP EDIDKIVHTY HTGKDVPEAT
FSIIDDDTKQ PMYACRVPVS EIIAEEYNCN IRRYVDNAPP PEPQDVRAHL HGGIPKKEVD
CLTHFWNNYK DLKEDCFSEK DNDYYQFSGK LDNRRSISEF INKHPGLQKR HEQFITSLSK
WWNKNHPVVE ALAHDPDNQH ESAGNVFLMR RTLIQSIEKL LSNQNILSFS QVRGAFANYV
DELKADFKSI AASGWGPELI PDEEILQSQF PQVLEEMEKY QSRIEELQSL FTTADDEDFE
DDEDTGVLPS SEVKDKKDSL KELNAAWKHE LKTLKALVAD LFAEIKAAGK LPGGEKKGFY
CTEGFAQNNP VFENGKKICE LAGRVNHSTD YTEKIETTIE NGITVYKQTQ YIEKALSRHK
ALEDELKELK KNIKAIENKR DELVESPRKK ISTDEARQVI LKRLKSMLLG TYTRYLQDDK
RACIKVVENL WDKYAVTAKE IEAERDKASS QLHEFLMELG YE
//
