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Database: UniProt
Entry: A0A1J0AB29_9CYAN
LinkDB: A0A1J0AB29_9CYAN
Original site: A0A1J0AB29_9CYAN 
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
//
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