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Database: UniProt
Entry: Q8R9Q4_CALS4
LinkDB: Q8R9Q4_CALS4
Original site: Q8R9Q4_CALS4 
ID   Q8R9Q4_CALS4            Unreviewed;       507 AA.
AC   Q8R9Q4;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 107.
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:AAM24756.1};
GN   OrderedLocusNames=TTE1547 {ECO:0000313|EMBL:AAM24756.1};
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068 {ECO:0000313|EMBL:AAM24756.1, ECO:0000313|Proteomes:UP000000555};
RN   [1] {ECO:0000313|EMBL:AAM24756.1, ECO:0000313|Proteomes:UP000000555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4
RC   {ECO:0000313|Proteomes:UP000000555};
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
RN   [2] {ECO:0007829|PDB:5YBB}
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE.
RX   PubMed=28973912; DOI=10.1073/pnas.1711754114;
RA   Liu Y.P., Tang Q., Zhang J.Z., Tian L.F., Gao P., Yan X.X.;
RT   "Structural basis underlying complex assembly and conformational transition
RT   of the type I R-M system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:11151-11156(2017).
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; AE008691; AAM24756.1; -; Genomic_DNA.
DR   RefSeq; WP_011025792.1; NZ_JANUCV010000001.1.
DR   PDB; 5YBB; X-ray; 3.20 A; A/B/C/E=1-507.
DR   PDBsum; 5YBB; -.
DR   AlphaFoldDB; Q8R9Q4; -.
DR   SMR; Q8R9Q4; -.
DR   STRING; 273068.TTE1547; -.
DR   REBASE; 6055; M.TteMI.
DR   KEGG; tte:TTE1547; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_018284_4_0_9; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000000555; Chromosome.
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:UniProtKB-KW.
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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5YBB}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AAM24756.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000555};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0007829|PDB:5YBB}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          10..135
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          149..455
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          473..504
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:5YBB"
FT   BINDING         202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:5YBB"
FT   BINDING         202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:5YBB"
FT   BINDING         233
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:5YBB"
FT   BINDING         233
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:5YBB"
FT   BINDING         260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:5YBB"
FT   BINDING         260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:5YBB"
FT   BINDING         261
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:5YBB"
FT   BINDING         261
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:5YBB"
SQ   SEQUENCE   507 AA;  58495 MW;  ECEBD3610551EF95 CRC64;
     MNGPQTRESL ANEIWRACDI MRRDNNCTGI MEYVEHLAWL LFLRFLDAQE EEWEAQAQIA
     GRPYTPIIDS EYRWRHWATK DWPADELLAF VHGRLIPYLR SLGGDPLRET IRSLFSERNV
     IVCASGYNLK DVIQIVNEIN FHSQDDIFTV SQVYEELLRR LGNENRLAGE FYTPRPVVRF
     VVELVDPQIG EAVYDPACGT CGFLVEAYLW MKQKERTIED HRILQERTFF GQEKKPVPAF
     LGLVNMMLHG VTVPRVMRRN TLEENIRNVS ERFDVVVTNP PFGGTEGRHI QQNFPIQSNA
     TELLFLQHIM KKLKPRDGAR CGMVVPEGTL FRGGAFAEVK RDLLEQFNLH TVVSLPPGTF
     APYSDVKTAL IFFERPGPTK EIWYYELPLP EGLKKFSKGN PIQDEHFEEA RKLWRGWDAY
     RKGLGPVEAC LSERSWIVPV EEVKKRGYDL TARNPNRSGG EELPSPVEIV AGLLEKEREI
     LSIMEELSEL LENEKGNSSR KNDEEEE
//
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