ID A0A1I1SKV9_9GAMM Unreviewed; 503 AA.
AC A0A1I1SKV9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN05660831_01637 {ECO:0000313|EMBL:SFD43670.1};
OS Thiohalospira halophila DSM 15071.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalospirales;
OC Thiohalospiraceae; Thiohalospira.
OX NCBI_TaxID=1123397 {ECO:0000313|EMBL:SFD43670.1, ECO:0000313|Proteomes:UP000198611};
RN [1] {ECO:0000313|EMBL:SFD43670.1, ECO:0000313|Proteomes:UP000198611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL3 {ECO:0000313|EMBL:SFD43670.1,
RC ECO:0000313|Proteomes:UP000198611};
RA de Groot N.N.;
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};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; FOMJ01000005; SFD43670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1SKV9; -.
DR STRING; 1123397.SAMN05660831_01637; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000198611; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000198611};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..113
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 123..416
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 503 AA; 57725 MW; F0005D06AF768431 CRC64;
MNAQTLVNKV WSFCHTLRDD GVGYGDYLEQ LTYLIFLKLA DEYSRPPYDR DIGIPAGYDW
PSLKRLKGAE LEAHYIETLR VLGQEGGMLG QIFMKAQNKI QDPAKLARVI EMIDAEDWAM
LDADVKGDLY EGLLEKNAED VKSGAGQYFT PRPLIEAMVE CIRPAPGKSI ADPACGTGGF
FLRAYDFITR EHELDGSEKR FLKHHTFHGN EIVAEARRMC LMNLFLHNIG DLDDQPTILS
TDALITPAPQ RYDYVLTNPP FGRKSSMTII NDDTGEQEKE DFVYERQDFW ATTSNKQLNF
VQHIRTMLKE NGQAAVVVPD NVLFEGGAGE TVRRKLLETT DLHTILRLPT GIFYAQGVKA
NVLFFDNRPG RAEPWTREVW FYDYRTNVHH TLKRKPLRLE HLQDFIRCYH PENRHERTET
WSEETPEGRW RRFTYEEILA RDKVSLDIFW LRDESLGDMD NLPEPEAIAE EIVENLEAGL
EGFRQVLASL EAEESTEPPS GKA
//
