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Database: UniProt
Entry: K9QD73_9NOSO
LinkDB: K9QD73_9NOSO
Original site: K9QD73_9NOSO 
ID   K9QD73_9NOSO            Unreviewed;       277 AA.
AC   K9QD73;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
GN   ORFNames=Nos7107_2420 {ECO:0000313|EMBL:AFY43029.1};
OS   Nostoc sp. PCC 7107.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY43029.1, ECO:0000313|Proteomes:UP000010381};
RN   [1] {ECO:0000313|EMBL:AFY43029.1, ECO:0000313|Proteomes:UP000010381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY43029.1,
RC   ECO:0000313|Proteomes:UP000010381};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished genome of Nostoc sp. PCC 7107.";
RL   Submitted (AUG-2012) 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         ECO:0000256|RuleBase:RU361257};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU361257}.
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DR   EMBL; CP003548; AFY43029.1; -; Genomic_DNA.
DR   RefSeq; WP_015113244.1; NC_019676.1.
DR   AlphaFoldDB; K9QD73; -.
DR   STRING; 317936.Nos7107_2420; -.
DR   REBASE; 57697; M.Nsp7107ORF2420P.
DR   KEGG; nos:Nos7107_2420; -.
DR   PATRIC; fig|317936.3.peg.2619; -.
DR   eggNOG; COG0338; Bacteria.
DR   HOGENOM; CLU_063430_0_0_3; -.
DR   InParanoid; K9QD73; -.
DR   OrthoDB; 9805629at2; -.
DR   Proteomes; UP000010381; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00571; dam; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
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:0000256|RuleBase:RU361257};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010381};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU361257};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361257}.
FT   BINDING         17
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         21
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         187
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ   SEQUENCE   277 AA;  31819 MW;  020A1BC7B55E7A5F CRC64;
     MVIQMLPETC PRPFLKWAGG KSRLIQQYLP YFPKFYQTYY EPFLGGGAVF FHLQPTTAIL
     TDINAELITT YRCVRDQVED LIGLLQEHKS KHNREYYYSV RSHPGRNDLE KAARLIYLNK
     TCYNGLYRVN SQGKFNVPLG SYKNPNICPA DLLRTASQAL SYCEIKQADF MNVLNYANSS
     DDFVFCDPPY HPISNTSYFT GYNGNSFGEQ DQTHLRDTCA ELANRGVKVM ICNSDCEFIR
     KIYKEINFNI YAIAASRSIN SNTKKRGIIS ELLITSY
//
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