ID A0A165Q9J7_9SPHN Unreviewed; 381 AA.
AC A0A165Q9J7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN ORFNames=A3736_12135 {ECO:0000313|EMBL:KZY55126.1};
OS Erythrobacter sp. HI0063.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1822240 {ECO:0000313|EMBL:KZY55126.1, ECO:0000313|Proteomes:UP000077326};
RN [1] {ECO:0000313|EMBL:KZY55126.1, ECO:0000313|Proteomes:UP000077326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0063 {ECO:0000313|EMBL:KZY55126.1,
RC ECO:0000313|Proteomes:UP000077326};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-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, ECO:0000256|RuleBase:RU362026}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZY55126.1}.
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DR EMBL; LWFF01000319; KZY55126.1; -; Genomic_DNA.
DR RefSeq; WP_067683579.1; NZ_LWFF01000319.1.
DR AlphaFoldDB; A0A165Q9J7; -.
DR OrthoDB; 9800801at2; -.
DR Proteomes; UP000077326; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR040843; RAMA.
DR InterPro; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF18755; RAMA; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KZY55126.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077326};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 49..268
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
FT DOMAIN 279..376
FT /note="RAMA"
FT /evidence="ECO:0000259|Pfam:PF18755"
SQ SEQUENCE 381 AA; 42817 MW; 70751DC16E542A72 CRC64;
MGVLETTKPR VVAREKEKSA GKQTVSLPLG QILDGDCVER LRQLPDASID LVFADPPYNL
QLGGDLNRPD GSHVDAVTDE WDRFESFLTY DDFTRAWLTE CKRVLKPDGG LWVIGSYHNI
YRVGAILQDL GFWILNDIVW RKSNPMPNFR GTRFTNAHET LLWCSQGEKA KYHFNYRAMK
TLNDELQMRS DWVLPICNGG ERLKENGHKV HPTQKPEALL YRVLLATTER GDVVLDPFFG
TGTTGAVAKR LGREWIGCER EGLYRDAARK RIARELPLDE SALTTMQAGR AAPKVAFGAL
VENGLIPPGT QVFDKQRRWT ATVRADGSLA HEKQTGSIHG LGKDLQNAPS CNGWTFWHFE
QDGAIKPIDA ARKLYLLAAE D
//
