ID A0A1J0AB29_9CYAN Unreviewed; 513 AA.
AC A0A1J0AB29;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN Name=hsdM {ECO:0000313|EMBL:APB33134.1};
GN ORFNames=GlitD10_0818 {ECO:0000313|EMBL:APB33134.1};
OS Gloeomargarita lithophora Alchichica-D10.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeomargaritales;
OC Gloeomargaritaceae; Gloeomargarita.
OX NCBI_TaxID=1188229 {ECO:0000313|EMBL:APB33134.1, ECO:0000313|Proteomes:UP000180235};
RN [1] {ECO:0000313|EMBL:APB33134.1, ECO:0000313|Proteomes:UP000180235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D10 {ECO:0000313|EMBL:APB33134.1,
RC ECO:0000313|Proteomes:UP000180235};
RA Moreira D., Tavera R., Benzerara K., Skouri-Panet F., Couradeau E.,
RA Gerard E., Loussert C., Novelo E., Zivanovic Y., Lopez-Garcia P.;
RT "Description of Gloeomargarita lithophora gen. nov., sp. nov., a thylakoid-
RT bearing basal-branching cyanobacterium with intracellular carbonates, and
RT proposal for Gloeomargaritales ord. nov.";
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};
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DR EMBL; CP017675; APB33134.1; -; Genomic_DNA.
DR RefSeq; WP_071453774.1; NZ_CP017675.1.
DR AlphaFoldDB; A0A1J0AB29; -.
DR STRING; 1188229.GlitD10_0818; -.
DR REBASE; 166411; M.GliD10ORF818P.
DR OrthoDB; 467945at2; -.
DR Proteomes; UP000180235; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR NCBIfam; TIGR00497; hsdM; 1.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000313|EMBL:APB33134.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000180235};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:APB33134.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..157
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 171..479
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 483..513
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 513 AA; 56727 MW; FB9551BC47B62B29 CRC64;
MTSIQQRAAL QRQIWQIAND VRGSVDGWDF KQYVLGTLFY RFISENFTSY IEAGDDSINY
AKLTDDIITD DIKEDAVKTK GYFIYPSQLF ANVVASANTN ESLNTDLAKI FAAIESSANG
YPSEMDIKGL FADFDTTSNR LGNTVKDKNL RLAAVLKGVA GLDFGDFEGS HIDLFGDAYE
FLISNYAANA GKSGGEFFTP QYVSRLIAQL AMHQQTGVNK IYDPACGSGS LLLQAKKHFD
AHLIEEGFYG QEINHTTYNL ARMNMFLHNI NYDKFNMQLG NTLTEPHFAD EKPFDAIVSN
PPYSVNWIGS DDPTLINDDR FAPAGVLAPK SKADFAFVLH CLSYLSSKGR AAIVCFPGIF
YRGGAEAQIR KYLVDNNYVE TVIALAPNLF FGTTIAVTIL VLSKRKHDTA TQFIDASGLF
KKETNNNTLT DDHIAAIMGV FDSKENVAHF ARSVTLEEIA ANDYNLSVSS YVEAKDTREV
VDINALNAKL KTTVAKIDRL RAEIDAIVAE IEA
//