ID A0A1Z4R313_9CYAN Unreviewed; 504 AA.
AC A0A1Z4R313;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=NIES4101_27860 {ECO:0000313|EMBL:BAZ36866.1};
OS Calothrix sp. NIES-4101.
OG Plasmid Plasmid5 dna {ECO:0000313|Proteomes:UP000290974}.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005461 {ECO:0000313|EMBL:BAZ36866.1, ECO:0000313|Proteomes:UP000290974};
RN [1] {ECO:0000313|EMBL:BAZ36866.1, ECO:0000313|Proteomes:UP000290974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4101 {ECO:0000313|EMBL:BAZ36866.1,
RC ECO:0000313|Proteomes:UP000290974};
RC PLASMID=Plasmid5 dna {ECO:0000313|Proteomes:UP000290974};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-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};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; AP018278; BAZ36866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4R313; -.
DR REBASE; 207567; M.Csp4101ORF27860P.
DR Proteomes; UP000290974; Plasmid Plasmid5 dna.
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 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:BAZ36866.1}; Plasmid {ECO:0000313|EMBL:BAZ36866.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000290974};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAZ36866.1}.
FT DOMAIN 4..90
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 153..473
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 504 AA; 57057 MW; BDA7D29F8B98D554 CRC64;
MFEQTFKNID DVLWKEAGCT TELDYTEQTS WLLFLKYLDD LEQERALEAE LVGKPYEFII
DEEHRWSVWA APKKADGTLD HDSALVGDDL IDYVSRKLFP YLQSFKQRAT SPDTIEYKIG
EIFSEIKNRF QSGYSLRDAL EYIDELRFRS QQEKHELSHL YEAKIKNMGN AGRNGGEYYT
PRPLIRAMIE VVKPKIGDRI YDGACGSAGF LCESYDYLRR GKLTTKELEI LQKHTFTGKE
KKSLAYVIAI MNMILHGIDA PNIIHTNTLT ENLSDIQDKN RFDVILANPP FGGKERKEVQ
QNFPIKTGET AFLFLQHFIK ILKVGGRAAV VIKNTFLSNS DNASKALREE LLSSCNLHTI
LDCPSGTFIG AGVKTVVLFF EKGKPFDSVQ GTPLFAQGKP LNEGMATRKI WYYQLDPGRN
MGKTNSLNDE DLREFVGLQA RFAETEKSWL VDIADVDRGT FDLSVKNPNK AEESALREPQ
EILDEIAVLD AESAEILAGI GGIL
//
